{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T19:16:15Z","timestamp":1786994175159,"version":"build-2736575974"},"reference-count":99,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004530","name":"Universiti Putra Malaysia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004530","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003093","name":"Government of Malaysia Ministry of Higher Education","doi-asserted-by":"publisher","award":["FRGS\/1\/2019\/STG05\/UPM\/02\/1"],"award-info":[{"award-number":["FRGS\/1\/2019\/STG05\/UPM\/02\/1"]}],"id":[{"id":"10.13039\/501100003093","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Microbial Pathogenesis"],"published-print":{"date-parts":[[2024,8]]},"DOI":"10.1016\/j.micpath.2024.106773","type":"journal-article","created":{"date-parts":[[2024,7,2]],"date-time":"2024-07-02T02:37:45Z","timestamp":1719887865000},"page":"106773","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Extracellular BSA-degrading SAPs in the rare pathogen Meyerozyma guilliermondii strain SO as potential virulence factors in candidiasis"],"prefix":"10.1016","volume":"193","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7171-0454","authenticated-orcid":false,"given":"Si Jie","family":"Lim","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noor Dina Muhd","family":"Noor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4027-5730","authenticated-orcid":false,"given":"Suriana","family":"Sabri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohd Shukuri Mohamad","family":"Ali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abu Bakar","family":"Salleh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0143-425X","authenticated-orcid":false,"given":"Siti Nurbaya","family":"Oslan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.micpath.2024.106773_bib1","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2019.103896","article-title":"Potential role of Candida albicans secreted aspartic protease 9 in serum induced-hyphal formation and interaction with oral epithelial cells","volume":"139","author":"Yang","year":"2020","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.micpath.2024.106773_bib2","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1080\/21505594.2019.1593776","article-title":"A unique aspartyl protease gene expansion in Talaromyces marneffei plays a role in growth inside host phagocytes","volume":"10","author":"Payne","year":"2019","journal-title":"Virulence"},{"key":"10.1016\/j.micpath.2024.106773_bib3","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1006051","article-title":"Integrated activity and genetic profiling of secreted peptidases in Cryptococcus neoformans reveals an aspartyl peptidase required for low pH survival and virulence","volume":"12","author":"Clarke","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.micpath.2024.106773_bib4","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2212533119","article-title":"The human pathobiont Malassezia furfur secreted protease Mfsap1 regulates cell dispersal and exacerbates skin inflammation","volume":"119","author":"Goh","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.micpath.2024.106773_bib5","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0006806","article-title":"Secreted aspartyl proteinase (PbSap) contributes to the virulence of Paracoccidioides brasiliensis infection","volume":"12","author":"Castilho","year":"2018","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.micpath.2024.106773_bib6","doi-asserted-by":"crossref","first-page":"424","DOI":"10.3390\/jof7060424","article-title":"Repositioning lopinavir, an HIV protease inhibitor, as a promising antifungal drug: lessons learned from Candida albicans\u2014in silico, in vitro and in vivo approaches","volume":"7","author":"Santos","year":"2021","journal-title":"J. Fungi"},{"key":"10.1016\/j.micpath.2024.106773_bib7","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.00312-20","article-title":"Vaccination with secreted aspartyl proteinase 2 protein from Candida parapsilosis can enhance survival of mice during C. tropicalis-mediated systemic candidiasis","volume":"88","author":"Shukla","year":"2020","journal-title":"Infect. Immun."},{"key":"10.1016\/j.micpath.2024.106773_bib8","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a019778","article-title":"The Candida pathogenic species complex","volume":"4","author":"Turner","year":"2014","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.micpath.2024.106773_bib9","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1074\/jbc.M509297200","article-title":"Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions","volume":"281","author":"Albrecht","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.micpath.2024.106773_bib10","first-page":"139","article-title":"Candida secreted aspartyl proteinases - expression and function during infection","volume":"11","author":"Naglik","year":"2004","journal-title":"Mikol. Lek."},{"key":"10.1016\/j.micpath.2024.106773_bib11","doi-asserted-by":"crossref","first-page":"4514","DOI":"10.1128\/iai.64.11.4514-4519.1996","article-title":"Evidence for degradation of gastrointestinal mucin by Candida albicans secretory aspartyl proteinase","volume":"64","author":"Colina","year":"1996","journal-title":"Infect. Immun."},{"key":"10.1016\/j.micpath.2024.106773_bib12","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1128\/IAI.00054-07","article-title":"Mucosal tissue invasion by Candida albicans is associated with E-cadherin degradation, mediated by transcription factor Rim101p and protease Sap5p","volume":"75","author":"Villar","year":"2007","journal-title":"Infect. Immun."},{"key":"10.1016\/j.micpath.2024.106773_bib13","doi-asserted-by":"crossref","first-page":"280","DOI":"10.3389\/fmicb.2016.00280","article-title":"Candida albicans agglutinin-like sequence (Als) family vignettes: a review of Als protein structure and function","volume":"7","author":"Hoyer","year":"2016","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib14","doi-asserted-by":"crossref","DOI":"10.1128\/mSphere.00484-19","article-title":"Functional characterization of secreted aspartyl proteases in Candida parapsilosis","volume":"4","author":"Singh","year":"2019","journal-title":"mSphere"},{"key":"10.1016\/j.micpath.2024.106773_bib15","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1111\/j.1574-695X.2009.00570.x","article-title":"Differential expression of Candida dubliniensis-secreted aspartyl proteinase genes (CdSAP1-4) under different physiological conditions and during infection of a keratinocyte culture","volume":"56","author":"Loaiza-Loeza","year":"2009","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib16","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1111\/j.1469-0691.2010.03248.x","article-title":"The role of secreted aspartyl proteinases in Candida tropicalis invasion and damage of oral mucosa","volume":"17","author":"Silva","year":"2011","journal-title":"Clin. Microbiol. Infect."},{"key":"10.1016\/j.micpath.2024.106773_bib17","doi-asserted-by":"crossref","DOI":"10.3390\/pathogens11090963","article-title":"Overview on the infections related to rare Candida Species","volume":"11","author":"Kumar","year":"2022","journal-title":"Pathogens"},{"key":"10.1016\/j.micpath.2024.106773_bib18","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1093\/jpids\/piaa043","article-title":"Invasive candidiasis due to Candida guilliermondii complex: epidemiology and antifungal susceptibility testing from a third-level pediatric center in Mexico","volume":"9","author":"Castillo-Bejarano","year":"2020","journal-title":"J. Pediatric Infect. Dis. Soc."},{"key":"10.1016\/j.micpath.2024.106773_bib19","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1007\/s42770-022-00813-2","article-title":"Meyerozyma guilliermondii species complex: review of current epidemiology, antifungal resistance, and mechanisms","volume":"53","author":"Ghasemi","year":"2022","journal-title":"Braz. J. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib20","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2020.553648","article-title":"A 5-year review of invasive fungal infection at an academic medical center","volume":"10","author":"Li","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib21","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112515","article-title":"Targeting fungal virulence factor by small molecules: structure-based discovery of novel secreted aspartic protease 2 (SAP2) inhibitors","volume":"201","author":"Li","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.micpath.2024.106773_bib22","first-page":"617","article-title":"A hybrid ligand and structure-based virtual screening of NCI compound library identifies potential SAPT1 inhibitors","volume":"26","author":"Sari","year":"2022","journal-title":"J. Res. Pharm."},{"key":"10.1016\/j.micpath.2024.106773_bib23","doi-asserted-by":"crossref","first-page":"2420","DOI":"10.1080\/21655979.2021.1933824","article-title":"Phloretin inhibited the pathogenicity and virulence factors against Candida albicans","volume":"12","author":"Liu","year":"2021","journal-title":"Bioengineered"},{"key":"10.1016\/j.micpath.2024.106773_bib24","doi-asserted-by":"crossref","first-page":"4490","DOI":"10.1016\/j.vaccine.2012.04.069","article-title":"A virosomal vaccine against candidal vaginitis: immunogenicity, efficacy and safety profile in animal models","volume":"30","author":"De Bernardis","year":"2012","journal-title":"Vaccine"},{"key":"10.1016\/j.micpath.2024.106773_bib25","doi-asserted-by":"crossref","DOI":"10.3390\/vaccines11020364","article-title":"Secreted aspartyl proteinases targeted multi-epitope vaccine design for Candida dubliniensis using immunoinformatics","volume":"11","author":"Akhtar","year":"2023","journal-title":"Vaccines"},{"key":"10.1016\/j.micpath.2024.106773_bib26","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1128\/EC.05200-11","article-title":"Rhb1 regulates the expression of secreted aspartic protease 2 through the TOR signaling pathway in Candida albicans","volume":"11","author":"Chen","year":"2012","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.micpath.2024.106773_bib27","doi-asserted-by":"crossref","DOI":"10.3390\/ijms221910633","article-title":"Candida albicans Sfp1 is involved in the cell wall and endoplasmic reticulum stress responses induced by human antimicrobial peptide LL-37","volume":"22","author":"Hsu","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.micpath.2024.106773_bib28","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.funbio.2009.12.003","article-title":"Amphotericin B resistance leads to enhanced proteinase and phospholipase activity and reduced germ tube formation in Candida albicans","volume":"114","author":"Kumar","year":"2010","journal-title":"Fungal Biol."},{"key":"10.1016\/j.micpath.2024.106773_bib29","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1093\/jac\/dki088","article-title":"Exposure of Candida albicans to antifungal agents affects expression of SAP2 and SAP9 secreted proteinase genes","volume":"55","author":"Copping","year":"2005","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.micpath.2024.106773_bib30","doi-asserted-by":"crossref","first-page":"892","DOI":"10.3109\/13693786.2013.824623","article-title":"Expression of SAP5 and SAP9 in Candida albicans biofilms: comparison of bloodstream isolates with isolates from other sources","volume":"51","author":"Joo","year":"2013","journal-title":"Med. Mycol."},{"key":"10.1016\/j.micpath.2024.106773_bib31","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.micpath.2018.12.028","article-title":"Correlation between antifungal resistance and virulence factors in Candida albicans recovered from vaginal specimens","volume":"128","author":"El-Houssaini","year":"2019","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.micpath.2024.106773_bib32","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.mycmed.2019.08.001","article-title":"Anti-fungal susceptibility and virulence factors of Candida spp. isolated from blood cultures","volume":"29","author":"Sriphannam","year":"2019","journal-title":"J. Mycol. Med."},{"key":"10.1016\/j.micpath.2024.106773_bib33","doi-asserted-by":"crossref","DOI":"10.3390\/pathogens10040466","article-title":"Virulence of clinical Candida isolates","volume":"10","author":"Mroczy\u0144ska","year":"2021","journal-title":"Pathogens"},{"key":"10.1016\/j.micpath.2024.106773_bib34","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1080\/21505594.2021.1908765","article-title":"Virulence of Candida auris from different clinical origins in Caenorhabditis elegans and Galleria mellonella host models","volume":"12","author":"Hernando-Ortiz","year":"2021","journal-title":"Virulence"},{"key":"10.1016\/j.micpath.2024.106773_bib35","first-page":"2817","article-title":"Segregation of proteinase-negative mutants from heterozygous Candida albicans","volume":"133","author":"Crandall","year":"1987","journal-title":"J. Gen. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib36","doi-asserted-by":"crossref","first-page":"327","DOI":"10.2174\/1573409918666220818120645","article-title":"Melianone inhibits secreted aspartic proteases (SAP), a virulence factor during hyphal formation in Candida albicans","volume":"18","author":"Veni","year":"2022","journal-title":"Curr. Comput. Aided Drug Des."},{"key":"10.1016\/j.micpath.2024.106773_bib37","first-page":"537","article-title":"Secretion of acid proteinases by different species of the genus Candida","volume":"255","author":"R\u00fcchel","year":"1983","journal-title":"Zentralbl. Bakteriol. Mikrobiol. Hyg. A."},{"key":"10.1016\/j.micpath.2024.106773_bib38","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1128\/iai.58.2.508-514.1990","article-title":"Comparative production and rapid purification of Candida acid proteinase from protein-supplemented cultures","volume":"58","author":"Ray","year":"1990","journal-title":"Infect. Immun."},{"key":"10.1016\/j.micpath.2024.106773_bib39","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2020.107674","article-title":"Biotechnological applications of the non-conventional yeast Meyerozyma guilliermondii","volume":"46","author":"Yan","year":"2021","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.micpath.2024.106773_bib40","first-page":"225","article-title":"Locally isolated yeasts from Malaysia: identification, phylogenetic study and characterization","volume":"59","author":"Oslan","year":"2012","journal-title":"Acta Bochimica Pol."},{"key":"10.1016\/j.micpath.2024.106773_bib41","doi-asserted-by":"crossref","DOI":"10.1155\/2015\/529059","article-title":"Expression and characterization of Geobacillus stearothermophilus SR74 recombinant \u03b1-amylase in Pichia pastoris","volume":"2015","author":"Gandhi","year":"2015","journal-title":"BioMed Res. Int."},{"key":"10.1016\/j.micpath.2024.106773_bib42","doi-asserted-by":"crossref","first-page":"3161","DOI":"10.15376\/biores.15.2.3161-3172","article-title":"Molecular expression of a recombinant thermostable bacterial amylase from Geobacillus stearothermophilus SR74 using methanol-free Meyerozyma guilliermondii strain SO yeast system","volume":"15","author":"Nasir","year":"2020","journal-title":"Bioresources"},{"key":"10.1016\/j.micpath.2024.106773_bib43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/07391102.2023.2300757","article-title":"Features of the rare pathogen Meyerozyma guilliermondii strain SO and comprehensive in silico analyses of its adherence-contributing virulence factor agglutinin-like sequences","author":"Lim","year":"2024","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.micpath.2024.106773_bib44","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2023.106025","article-title":"Enolase in Meyerozyma guilliermondii strain SO: sequential and structural insights of MgEno4581 as a putative virulence factor and host-fungal interactions through comprehensive in silico approaches","volume":"176","author":"Amran","year":"2023","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.micpath.2024.106773_bib45","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/s43042-023-00384-3","article-title":"In silico identification of prospective virulence factors associated with candidiasis in Meyerozyma guilliermondii strain SO from genome dataset, Egypt","volume":"24","author":"Zainudin","year":"2023","journal-title":"J. Med. Hum. Genet."},{"key":"10.1016\/j.micpath.2024.106773_bib46","doi-asserted-by":"crossref","first-page":"777","DOI":"10.47836\/pjst.30.1.42","article-title":"Determination of putative vacuolar proteases, PEP4 and PRB1 in a novel yeast expression host Meyerozyma guilliermondii strain SO using bioinformatics tools","volume":"30","author":"Lorrine","year":"2022","journal-title":"Pertanika J. Sci. Technol."},{"key":"10.1016\/j.micpath.2024.106773_bib47","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000217","article-title":"The hyphal-associated adhesin and invasin Als3 of Candida albicans mediates iron acquisition from host ferritin","volume":"4","author":"Almeida","year":"2008","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.micpath.2024.106773_bib48","doi-asserted-by":"crossref","first-page":"e970","DOI":"10.1002\/mbo3.970","article-title":"The adaptive response to iron involves changes in energetic strategies in the pathogen Candida albicans","volume":"9","author":"Duval","year":"2020","journal-title":"Microbiologyopen"},{"key":"10.1016\/j.micpath.2024.106773_bib49","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/s41587-021-01156-3","article-title":"SignalP 6.0 predicts all five types of signal peptides using protein language models","volume":"40","author":"Teufel","year":"2022","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.micpath.2024.106773_bib50","doi-asserted-by":"crossref","first-page":"3387","DOI":"10.1093\/bioinformatics\/btx431","article-title":"DeepLoc: prediction of protein subcellular localization using deep learning","volume":"33","author":"Almagro Armenteros","year":"2017","journal-title":"Bioinformatics"},{"key":"10.1016\/j.micpath.2024.106773_bib51","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1186\/1471-2105-9-392","article-title":"PredGPI: a GPI-anchor predictor","volume":"9","author":"Pierleoni","year":"2008","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.micpath.2024.106773_bib52","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.micpath.2024.106773_bib53","doi-asserted-by":"crossref","first-page":"3969","DOI":"10.1128\/AEM.65.9.3969-3975.1999","article-title":"Purification and characterization of an extracellular protease from the fish pathogen Yersinia ruckeri and effect of culture conditions on production","volume":"65","author":"Secades","year":"1999","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib54","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.3389\/fmicb.2018.01383","article-title":"Fonsecaea pedrosoi sclerotic cells: secretion of aspartic-type peptidase and susceptibility to peptidase inhibitors","volume":"9","author":"Palmeira","year":"2018","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib55","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.micpath.2024.106773_bib56","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0050300","article-title":"PROSPER: an integrated feature-based tool for predicting protease substrate cleavage sites","volume":"7","author":"Song","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.micpath.2024.106773_bib57","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1111\/j.1439-0507.2009.01793.x","article-title":"Enhancement of secretory aspartyl protease production in biofilms of Candida albicans exposed to sub-inhibitory concentrations of fluconazole","volume":"54","author":"Mores","year":"2011","journal-title":"Mycoses"},{"key":"10.1016\/j.micpath.2024.106773_bib58","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1248\/bpb.30.1813","article-title":"Candida albicans biofilms produce more secreted aspartyl protease than the planktonic cells","volume":"30","author":"Mendes","year":"2007","journal-title":"Biol. Pharm. Bull."},{"key":"10.1016\/j.micpath.2024.106773_bib59","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25094775","article-title":"Secreted aspartic proteinases: key factors in Candida infections and host-pathogen interactions","volume":"25","author":"Bras","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.micpath.2024.106773_bib60","article-title":"Bibliometric analysis and thematic review of Candida pathogenesis: Fundamental omics to applications as potential antifungal drugs and vaccines","author":"Lim","year":"2023","journal-title":"Med. Mycol."},{"key":"10.1016\/j.micpath.2024.106773_bib61","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23115895","article-title":"Virulence factors of Candida spp. and host immune response important in the pathogenesis of vulvovaginal candidiasis","volume":"23","author":"Czechowicz","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.micpath.2024.106773_bib62","doi-asserted-by":"crossref","first-page":"313","DOI":"10.2174\/1389203720666190722152415","article-title":"Virulence factors in Candida species","volume":"21","author":"Staniszewska","year":"2020","journal-title":"Curr. Protein Pept. Sci."},{"key":"10.1016\/j.micpath.2024.106773_bib63","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1002\/jps.20625","article-title":"BSA degradation under acidic conditions: a model for protein instability during release from PLGA delivery systems","volume":"95","author":"Estey","year":"2006","journal-title":"J. Pharmaceut. Sci."},{"key":"10.1016\/j.micpath.2024.106773_bib64","series-title":"The Yeasts","first-page":"9","article-title":"Yeasts pathogenic to humans","author":"Cooper","year":"2011"},{"key":"10.1016\/j.micpath.2024.106773_bib65","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.00099-17","article-title":"Candida guilliermondii complex is characterized by high antifungal resistance but low mortality in 22 cases of candidemia","volume":"61","author":"Marcos-Zambrano","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.micpath.2024.106773_bib66","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1128\/MMBR.67.3.400-428.2003","article-title":"Candida albicans secreted aspartyl proteinases in virulence and pathogenesis","volume":"67","author":"Naglik","year":"2003","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.micpath.2024.106773_bib67","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00724-15","article-title":"Secretory aspartyl proteinases cause vaginitis and can mediate vaginitis caused by Candida albicans in mice","volume":"6","author":"Pericolini","year":"2015","journal-title":"mBio"},{"key":"10.1016\/j.micpath.2024.106773_bib68","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1186\/s12866-015-0394-8","article-title":"Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans","volume":"15","author":"Kozik","year":"2015","journal-title":"BMC Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib69","doi-asserted-by":"crossref","first-page":"403","DOI":"10.18388\/abp.2016_1318","article-title":"The action of ten secreted aspartic proteases of pathogenic yeast Candida albicans on major human salivary antimicrobial peptide, histatin 5","volume":"63","author":"Bochenska","year":"2016","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.micpath.2024.106773_bib70","doi-asserted-by":"crossref","DOI":"10.1080\/19490976.2021.2004798","article-title":"Membrane protective role of autophagic machinery during infection of epithelial cells by Candida albicans","volume":"14","author":"Lapaquette","year":"2022","journal-title":"Gut Microb."},{"key":"10.1016\/j.micpath.2024.106773_bib71","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.13238","article-title":"Protective effect of fungal extracellular vesicles against murine candidiasis","volume":"22","author":"Vargas","year":"2020","journal-title":"Cell Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib72","doi-asserted-by":"crossref","first-page":"7963","DOI":"10.1016\/S0021-9258(18)92922-4","article-title":"Three proteolytic systems in the yeast Saccharomyces cerevisiae","volume":"266","author":"Jones","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.micpath.2024.106773_bib73","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1128\/EC.4.8.1364-1374.2005","article-title":"Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae","volume":"4","author":"Krysan","year":"2005","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.micpath.2024.106773_bib74","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.bbamcr.2016.12.009","article-title":"Proteolytic processing of the Saccharomyces cerevisiae cell wall protein Scw4 regulates its activity and influences its covalent binding to glucan","volume":"1864","author":"Grbavac","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"10.1016\/j.micpath.2024.106773_bib75","doi-asserted-by":"crossref","first-page":"6410","DOI":"10.1074\/jbc.M117.813741","article-title":"Aspartyl proteases in Candida glabrata are required for suppression of the host innate immune response","volume":"293","author":"Rasheed","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.micpath.2024.106773_bib76","doi-asserted-by":"crossref","first-page":"6239","DOI":"10.1021\/jf200348n","article-title":"Evidence for an extracellular acid proteolytic activity secreted by living cells of Saccharomyces cerevisiae PlR1: impact on grape proteins","volume":"59","author":"Younes","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.micpath.2024.106773_bib77","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1002\/jobm.200900068","article-title":"Spontaneous and protein-induced secretion of proteinases from Saccharomyces cerevisiae","volume":"49","author":"Kurucov\u00e1","year":"2009","journal-title":"J. Basic Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib78","doi-asserted-by":"crossref","DOI":"10.1016\/j.micres.2021.126831","article-title":"The impact of carbon and nitrogen catabolite repression in microorganisms","volume":"251","author":"Nair","year":"2021","journal-title":"Microbiol. Res."},{"key":"10.1016\/j.micpath.2024.106773_bib79","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1111\/mmi.13887","article-title":"Overview of carbon and nitrogen catabolite metabolism in the virulence of human pathogenic fungi","volume":"107","author":"Ries","year":"2018","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib80","doi-asserted-by":"crossref","first-page":"2250","DOI":"10.1128\/jb.173.7.2250-2255.1991","article-title":"Evolutionary relationships among pathogenic Candida species and relatives","volume":"173","author":"Barns","year":"1991","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.micpath.2024.106773_bib81","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0092734","article-title":"Regulatory networks controlling nitrogen sensing and uptake in Candida albicans","volume":"9","author":"Ramachandra","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.micpath.2024.106773_bib82","doi-asserted-by":"crossref","DOI":"10.3791\/58192-v","article-title":"Saccharomyces cerevisiae exponential growth kinetics in batch culture to analyze respiratory and fermentative metabolism","author":"Olivares-Marin","year":"2018","journal-title":"J. Vis. Exp."},{"key":"10.1016\/j.micpath.2024.106773_bib83","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1007\/s002530051659","article-title":"Proteolytic stability of recombinant human serum albumin secreted in the yeast Saccharomyces cerevisiae","volume":"53","author":"Kang","year":"2000","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.micpath.2024.106773_bib84","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jbiotec.2010.06.014","article-title":"Multiple-yapsin-deficient mutant strains for high-level production of intact recombinant proteins in Saccharomyces cerevisiae","volume":"149","author":"Cho","year":"2010","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.micpath.2024.106773_bib85","doi-asserted-by":"crossref","first-page":"9435","DOI":"10.1128\/MCB.25.21.9435-9446.2005","article-title":"Divergence of Stp1 and Stp2 transcription factors in Candida albicans places virulence factors required for proper nutrient acquisition under amino acid control","volume":"25","author":"Mart\u00ednez","year":"2005","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.micpath.2024.106773_bib86","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1128\/EC.3.1.135-143.2004","article-title":"Candida albicans Csy1p is a nutrient sensor important for activation of amino acid uptake and hyphal morphogenesis","volume":"3","author":"Brega","year":"2004","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.micpath.2024.106773_bib87","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1046\/j.1365-2958.2003.03845.x","article-title":"An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans","volume":"51","author":"Mart\u00ednez","year":"2004","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib88","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1128\/jb.84.4.869-870.1962","article-title":"Minor element composition of yeast extract","volume":"84","author":"Grant","year":"1962","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.micpath.2024.106773_bib89","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.funbio.2020.03.001","article-title":"Multi trace element profiling in pathogenic and non-pathogenic fungi","volume":"124","author":"Wehmeier","year":"2020","journal-title":"Fungal Biol."},{"key":"10.1016\/j.micpath.2024.106773_bib90","doi-asserted-by":"crossref","first-page":"3192","DOI":"10.1039\/jr9530003192","article-title":"The stability of transition-metal complexes","author":"Irving","year":"1953","journal-title":"J. Chem. Soc."},{"key":"10.1016\/j.micpath.2024.106773_bib91","article-title":"Albumin neutralizes hydrophobic toxins and modulates Candida albicans pathogenicity","volume":"12","author":"Sophie","year":"2021","journal-title":"mBio"},{"key":"10.1016\/j.micpath.2024.106773_bib92","doi-asserted-by":"crossref","first-page":"160","DOI":"10.3109\/14756366.2011.627508","article-title":"The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir","volume":"27","author":"Dost\u00e1l","year":"2012","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.micpath.2024.106773_bib93","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s11046-012-9522-2","article-title":"In vitro Candida albicans biofilm induced proteinase activity and SAP8 expression correlates with in vivo denture stomatitis severity","volume":"174","author":"Ramage","year":"2012","journal-title":"Mycopathologia"},{"key":"10.1016\/j.micpath.2024.106773_bib94","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1186\/1471-2180-10-114","article-title":"Real-time PCR expression profiling of genes encoding potential virulence factors in Candida albicans biofilms: identification of model-dependent and -independent gene expression","volume":"10","author":"Nailis","year":"2010","journal-title":"BMC Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib95","doi-asserted-by":"crossref","first-page":"794","DOI":"10.3389\/fmicb.2020.00794","article-title":"The transcription factor Stp2 is important for Candida albicans biofilm establishment and sustainability","volume":"11","author":"B\u00f6ttcher","year":"2020","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.micpath.2024.106773_bib96","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/s41522-022-00341-9","article-title":"Impaired amino acid uptake leads to global metabolic imbalance of Candida albicans biofilms","volume":"8","author":"B\u00f6ttcher","year":"2022","journal-title":"Npj Biofilms Microbiomes"},{"key":"10.1016\/j.micpath.2024.106773_bib97","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1111\/1567-1364.12068","article-title":"Clinical isolates and laboratory reference Candida species and strains have varying abilities to form biofilms","volume":"13","author":"Alnuaimi","year":"2013","journal-title":"FEMS Yeast Res."},{"key":"10.1016\/j.micpath.2024.106773_bib98","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000828","article-title":"Dispersion as an important step in the Candida albicans biofilm developmental cycle","volume":"6","author":"Uppuluri","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.micpath.2024.106773_bib99","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01338-18","article-title":"Candida albicans dispersed cells are developmentally distinct from biofilm and planktonic cells","volume":"9","author":"Uppuluri","year":"2018","journal-title":"mBio"}],"container-title":["Microbial Pathogenesis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0882401024002407?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0882401024002407?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,7,20]],"date-time":"2024-07-20T14:45:56Z","timestamp":1721486756000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0882401024002407"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,8]]},"references-count":99,"alternative-id":["S0882401024002407"],"URL":"https:\/\/doi.org\/10.1016\/j.micpath.2024.106773","relation":{},"ISSN":["0882-4010"],"issn-type":[{"value":"0882-4010","type":"print"}],"subject":[],"published":{"date-parts":[[2024,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Extracellular BSA-degrading SAPs in the rare pathogen Meyerozyma guilliermondii strain SO as potential virulence factors in candidiasis","name":"articletitle","label":"Article Title"},{"value":"Microbial Pathogenesis","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.micpath.2024.106773","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"106773"}}