{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T11:39:09Z","timestamp":1784547549430,"version":"3.55.0"},"reference-count":65,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2022,5,20]],"date-time":"2022-05-20T00:00:00Z","timestamp":1653004800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["FC 2015-02-834"],"award-info":[{"award-number":["FC 2015-02-834"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["Ciencia de Frontera 2019-6380"],"award-info":[{"award-number":["Ciencia de Frontera 2019-6380"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["INFR-2016-01-269833"],"award-info":[{"award-number":["INFR-2016-01-269833"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["CONACYT-M\u00e9xico"],"award-info":[{"award-number":["CONACYT-M\u00e9xico"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Red Tem\u00e1tica Glicociencia en Salud (CONACYT-M\u00e9xico)","award":["FC 2015-02-834"],"award-info":[{"award-number":["FC 2015-02-834"]}]},{"name":"Red Tem\u00e1tica Glicociencia en Salud (CONACYT-M\u00e9xico)","award":["Ciencia de Frontera 2019-6380"],"award-info":[{"award-number":["Ciencia de Frontera 2019-6380"]}]},{"name":"Red Tem\u00e1tica Glicociencia en Salud (CONACYT-M\u00e9xico)","award":["INFR-2016-01-269833"],"award-info":[{"award-number":["INFR-2016-01-269833"]}]},{"name":"Red Tem\u00e1tica Glicociencia en Salud (CONACYT-M\u00e9xico)","award":["CONACYT-M\u00e9xico"],"award-info":[{"award-number":["CONACYT-M\u00e9xico"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JoF"],"abstract":"<jats:p>The fungal cell wall is an attractive structure to look for new antifungal drug targets and for understanding the host-fungus interaction. Sporothrix schenckii is one of the main causative agents of both human and animal sporotrichosis and currently is the species most studied of the Sporothrix genus. The cell wall of this organism has been previously analyzed, and rhamnoconjugates are signature molecules found on the surface of both mycelia and yeast-like cells. Similar to other reactions where sugars are covalently linked to other sugars, lipids, or proteins, the rhamnosylation process in this organism is expected to involve glycosyltransferases with the ability to transfer rhamnose from a sugar donor to the acceptor molecule, i.e., rhamnosyltransferases. However, no obvious rhamnosyltransferase has thus far been identified within the S. schenckii proteome or genome. Here, using a Hidden Markov Model profile strategy, we found within the S. schenckii genome five putative genes encoding for rhamnosyltransferases. Expression analyses indicated that only two of them, named RHT1 and RHT2, were significantly expressed in yeast-like cells and during interaction with the host. These two genes were heterologously expressed in Escherichia coli, and the purified recombinant proteins showed rhamnosyltransferase activity, dependent on the presence of UDP-rhamnose as a sugar donor. To the best of our knowledge, this is the first report about rhamnosyltransferases in S. schenckii.<\/jats:p>","DOI":"10.3390\/jof8050529","type":"journal-article","created":{"date-parts":[[2022,5,20]],"date-time":"2022-05-20T13:56:12Z","timestamp":1653054972000},"page":"529","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["The Search for Cryptic L-Rhamnosyltransferases on the Sporothrix schenckii Genome"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6973-0595","authenticated-orcid":false,"given":"H\u00e9ctor M.","family":"Mora-Montes","sequence":"first","affiliation":[{"name":"Departamento de Biolog\u00eda, Divisi\u00f3n de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta S\/N, Col. Noria Alta, Guanajuato, Guanajuato 360501, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2086-5362","authenticated-orcid":false,"given":"Karina","family":"Garc\u00eda-Guti\u00e9rrez","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda, Divisi\u00f3n de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta S\/N, Col. Noria Alta, Guanajuato, Guanajuato 360501, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura C.","family":"Garc\u00eda-Carnero","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda, Divisi\u00f3n de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta S\/N, Col. Noria Alta, Guanajuato, Guanajuato 360501, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy E.","family":"Lozoya-P\u00e9rez","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda, Divisi\u00f3n de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta S\/N, Col. Noria Alta, Guanajuato, Guanajuato 360501, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2780-5223","authenticated-orcid":false,"given":"Jorge H.","family":"Ramirez-Prado","sequence":"additional","affiliation":[{"name":"Unidad de Biotecnolog\u00eda, Centro de Investigaci\u00f3n Cient\u00edfica de Yucat\u00e1n, A.C., Calle 43 No. 130, Col. Chuburn\u00e1 de Hidalgo, M\u00e9rida, Yucatan 97205, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,5,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"165rv113","DOI":"10.1126\/scitranslmed.3004404","article-title":"Hidden killers: Human fungal infections","volume":"4","author":"Brown","year":"2012","journal-title":"Sci. Transl. Med."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"e00449-20","DOI":"10.1128\/mBio.00449-20","article-title":"Threats posed by the fungal kingdom to humans, wildlife, and agriculture","volume":"11","author":"Fisher","year":"2020","journal-title":"mBio"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.jgar.2017.10.024","article-title":"Does the use of antifungal agents in agriculture and food foster polyene resistance development? A reason for concern","volume":"13","author":"Dalhoff","year":"2018","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Brauer, V.S., Rezende, C.P., Pessoni, A.M., De Paula, R.G., Rangappa, K.S., Nayaka, S.C., Gupta, V.K., and Almeida, F. (2019). Antifungal agents in agriculture: Friends and foes of public health. Biomolecules, 9.","DOI":"10.3390\/biom9100521"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Du, H., Bing, J., Hu, T., Ennis, C.L., Nobile, C.J., and Huang, G. (2020). Candida auris: Epidemiology, biology, antifungal resistance, and virulence. PLoS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008921"},{"key":"ref_6","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":"ref_7","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.fgb.2014.09.004","article-title":"Virulence mechanisms and Cryptococcus neoformans pathogenesis","volume":"78","author":"Alspaugh","year":"2015","journal-title":"Fungal Genet. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"692491","DOI":"10.3389\/fmicb.2021.692491","article-title":"It takes two to tango: How a dysregulation of the innate immunity, coupled with Candida virulence, triggers VVC onset","volume":"12","author":"Ardizzoni","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"295","DOI":"10.2174\/1389203720666191007103004","article-title":"Virulence factors in Sporothrix schenckii, one of the causative agents of sporotrichosis","volume":"21","author":"Romeo","year":"2020","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Lopes-Bezerra, L.M., Walker, L.A., Ni\u00f1o-Vega, G., Mora-Montes, H.M., Neves, G.W.P., Villalobos-Duno, H., Barreto, L., Garcia, K., Franco, B., and Mart\u00ednez-\u00c1lvarez, J.A. (2018). Cell walls of the dimorphic fungal pathogens Sporothrix schenckii and Sporothrix brasiliensis exhibit bilaminate structures and sloughing of extensive and intact layers. PLoS Negl. Trop. Dis., 12.","DOI":"10.1371\/journal.pntd.0006169"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1007\/s12281-012-0109-7","article-title":"Role of the fungal cell wall in pathogenesis and antifungal resistance","volume":"6","year":"2012","journal-title":"Curr. Fungal Infect. Rep."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/mmy.39.1.1.8-0","article-title":"Molecular organization of the cell wall of Candida albicans","volume":"39","author":"Klis","year":"2001","journal-title":"Med. Mycol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1146\/annurev-micro-030117-020406","article-title":"The cell wall of the human fungal pathogen Aspergillus fumigatus: Biosynthesis, organization, immune response, and virulence","volume":"71","author":"Beauvais","year":"2017","journal-title":"Ann. Rev. Microbiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"843","DOI":"10.3389\/fmicb.2017.00843","article-title":"Sporothrix schenckii sensu stricto and Sporothrix brasiliensis are differentially recognized by human peripheral blood mononuclear cells","volume":"8","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Lozoya-P\u00e9rez, N.E., Clavijo-Giraldo, D.M., Mart\u00ednez-Duncker, I., Garc\u00eda-Carnero, L.C., L\u00f3pez-Ram\u00edrez, L.A., Ni\u00f1o-Vega, G.A., and Mora-Montes, H.M. (2020). Influences of the culturing media in the virulence and cell wall of Sporothrix schenckii, Sporothrix brasiliensis, and Sporothrix globosa. J. Fungi, 6.","DOI":"10.3390\/jof6040323"},{"key":"ref_16","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":"ref_17","first-page":"1050","article-title":"Contribution of aspartic proteases in Candida virulence. protease inhibitors against candida infections","volume":"18","author":"Staniszewska","year":"2017","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_18","first-page":"243","article-title":"Sporothrix schenckii cell wall peptidorhamnomannans","volume":"2","year":"2011","journal-title":"Front. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Carnero, L.C., Salinas-Mar\u00edn, R., Lozoya-P\u00e9rez, N.E., Wrobel, K., Wrobel, K., Mart\u00ednez-Duncker, I., Ni\u00f1o-Vega, G.A., and Mora-Montes, H.M. (2021). The heat shock protein 60 and Pap1 participate in the Sporothrix schenckii-host interaction. J. Fungi, 7.","DOI":"10.3390\/jof7110960"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.2217\/fmb.09.88","article-title":"Protein glycosylation in Candida","volume":"4","author":"Gow","year":"2009","journal-title":"Future Microbiol."},{"key":"ref_21","first-page":"67","article-title":"Silencing of OCH1 unveils the role of Sporothrix schenckii N-linked glycans during the host-fungus interaction","volume":"12","author":"Jannuzzi","year":"2019","journal-title":"Infect. Drug Resist."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.fgb.2014.06.011","article-title":"Fungal model systems and the elucidation of pathogenicity determinants","volume":"70","author":"Nogueira","year":"2014","journal-title":"Fungal Genet. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"G\u00f3mez-Gaviria, M., Vargas-Mac\u00edas, A.P., Garc\u00eda-Carnero, L.C., Mart\u00ednez-Duncker, I., and Mora-Montes, H.M. (2021). Role of protein glycosylation in interactions of medically relevant fungi with the host. J. Fungi, 7.","DOI":"10.3390\/jof7100875"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1111\/mpp.12401","article-title":"Rhamnose synthase activity is required for pathogenicity of the vascular wilt fungus Verticillium dahliae","volume":"18","author":"Santhanam","year":"2017","journal-title":"Mol. Plant Pathol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1111\/j.1439-0507.2011.02105.x","article-title":"Glycoconjugates and polysaccharides from the Scedosporium\/Pseudallescheria boydii complex: Structural characterisation, involvement in cell differentiation, cell recognition and virulence","volume":"54","author":"Lopes","year":"2011","journal-title":"Mycoses"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"100058","DOI":"10.1016\/j.tcsw.2021.100058","article-title":"Disruption of protein rhamnosylation affects the Sporothrix schenckii-host interaction","volume":"7","year":"2021","journal-title":"Cell Surf."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"726958","DOI":"10.3389\/fmicb.2021.726958","article-title":"Comparison of cell wall polysaccharide composition and structure between strains of Sporothrix schenckii and Sporothrix brasiliensis","volume":"12","author":"Barreto","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1093\/mmy\/myx103","article-title":"Sporotrichosis between 1898 and 2017: The evolution of knowledge on a changeable disease and on emerging etiological agents","volume":"56","author":"Zhang","year":"2018","journal-title":"Med. Mycol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"fov065","DOI":"10.1093\/femsyr\/fov065","article-title":"Current progress in the biology of members of the Sporothrix schenckii complex following the genomic era","volume":"15","year":"2015","journal-title":"FEMS Yeast Res."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Teixeira, M.M., de Almeida, L.G., Kubitschek-Barreira, P., Alves, F.L., Kioshima, E.S., Abadio, A.K., Fernandes, L., Derengowski, L.S., Ferreira, K.S., and Souza, R.C. (2014). Comparative genomics of the major fungal agents of human and animal Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis. BMC Genom., 15.","DOI":"10.1186\/1471-2164-15-943"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/978-3-030-58971-4_6","article-title":"Recent progress in structural studies on the GT-C superfamily of protein glycosyltransferases","volume":"96","author":"Bohl","year":"2021","journal-title":"Sub-Cell. Biochem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.sbi.2012.06.007","article-title":"Recent structures, evolution and mechanisms of glycosyltransferases","volume":"22","author":"Breton","year":"2012","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"29r","DOI":"10.1093\/glycob\/cwj016","article-title":"Structures and mechanisms of glycosyltransferases","volume":"16","author":"Breton","year":"2006","journal-title":"Glycobiology"},{"key":"ref_34","first-page":"mgen000445","article-title":"Transcriptome-wide expression profiling of Sporothrix schenckii yeast and mycelial forms and the establishment of the Sporothrix Genome DataBase","volume":"6","author":"Giosa","year":"2020","journal-title":"Microb. Genom."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"D20","DOI":"10.1093\/nar\/gkab1112","article-title":"Database resources of the National Center for Biotechnology Information","volume":"50","author":"Sayers","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"D412","DOI":"10.1093\/nar\/gkaa913","article-title":"Pfam: The protein families database in 2021","volume":"49","author":"Mistry","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/nar\/28.1.235","article-title":"The Protein Data Bank","volume":"28","author":"Berman","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"D437","DOI":"10.1093\/nar\/gkaa1038","article-title":"RCSB Protein Data Bank: Powerful new tools for exploring 3D structures of biological macromolecules for basic and applied research and education in fundamental biology, biomedicine, biotechnology, bioengineering and energy sciences","volume":"49","author":"Burley","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"ref_40","first-page":"D570","article-title":"MGnify: The microbiome analysis resource in 2020","volume":"48","author":"Mitchell","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"D170","DOI":"10.1093\/nar\/gkw1081","article-title":"Uniclust databases of clustered and deeply annotated protein sequences and alignments","volume":"45","author":"Mirdita","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2856","DOI":"10.1093\/bioinformatics\/bty1057","article-title":"MMseqs2 desktop and local web server app for fast, interactive sequence searches","volume":"35","author":"Mirdita","year":"2019","journal-title":"Bioinformatics"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Mirdita, M., Sch\u00fctze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., and Steinegger, M. (2022). ColabFold-Making protein folding accessible to all. bioRxiv.","DOI":"10.1101\/2021.08.15.456425"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1093\/bib\/bbx108","article-title":"MAFFT online service: Multiple sequence alignment, interactive sequence choice and visualization","volume":"20","author":"Katoh","year":"2019","journal-title":"Brief. Bioinform."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1676","DOI":"10.3389\/fmicb.2017.01676","article-title":"The Sporothrix schenckii gene encoding for the ribosomal protein L6 has constitutive and stable expression and works as an endogenous control in gene expression analysis","volume":"8","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1016\/j.funbio.2012.06.002","article-title":"Isolation and functional characterization of Sporothrix schenckii ROT2, the encoding gene for the endoplasmic reticulum glucosidase II","volume":"116","author":"Lee","year":"2012","journal-title":"Fungal Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1080\/15257770.2016.1184277","article-title":"Purification of single-stranded cDNA based on RNA degradation treatment and adsorption chromatography","volume":"35","author":"Franco","year":"2016","journal-title":"Nucleosides Nucleotides Nucleic Acids"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"397","DOI":"10.2217\/fmb-2018-0295","article-title":"Analysis of some immunogenic properties of the recombinant Sporothrix schenckii Gp70 expressed in Escherichia coli","volume":"14","author":"Curty","year":"2019","journal-title":"Future Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1038\/nprot.2006.288","article-title":"Silver staining of proteins in polyacrylamide gels","volume":"1","author":"Chevallet","year":"2006","journal-title":"Nat. Protoc."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"14932","DOI":"10.1074\/jbc.M611498200","article-title":"Identification of a flavonol 7-O-rhamnosyltransferase gene determining flavonoid pattern in Arabidopsis by transcriptome coexpression analysis and reverse genetics","volume":"282","author":"Tohge","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1093\/glycob\/cwh091","article-title":"Hydrolysis of Man9GlcNAc2 and Man8GlcNAc2 oligosaccharides by a purified \u03b1-mannosidase from Candida albicans","volume":"14","author":"Zinker","year":"2004","journal-title":"Glycobiology"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1016\/j.fgb.2008.08.003","article-title":"Functional analysis of Candida albicans GPI-anchored proteins: Roles in cell wall integrity and caspofungin sensitivity","volume":"45","author":"Plaine","year":"2008","journal-title":"Fungal Genet. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/j.resmic.2017.07.005","article-title":"Saccharomyces cerevisiae KTR4, KTR5 and KTR7 encode mannosyltransferases differentially involved in the N- and O-linked glycosylation pathways","volume":"168","year":"2017","journal-title":"Res. Microbiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0022-2836(03)00307-3","article-title":"An evolving hierarchical family classification for glycosyltransferases","volume":"328","author":"Coutinho","year":"2003","journal-title":"J. Mol. Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.sbi.2014.08.012","article-title":"Advances in understanding glycosyltransferases from a structural perspective","volume":"28","author":"Gloster","year":"2014","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"17649","DOI":"10.1073\/pnas.1108484108","article-title":"Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity","volume":"108","author":"Chang","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/j.str.2008.03.010","article-title":"Solution structure of Alg13: The sugar donor subunit of a yeast N-acetylglucosamine transferase","volume":"16","author":"Wang","year":"2008","journal-title":"Structure"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1111\/tpj.14321","article-title":"Crystal structures of rhamnosyltransferase UGT89C1 from Arabidopsis thaliana reveal the molecular basis of sugar donor specificity for UDP-\u03b2-l-rhamnose and rhamnosylation mechanism","volume":"99","author":"Zong","year":"2019","journal-title":"Plant J. Cell Mol. Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1042\/bj3260929u","article-title":"A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities","volume":"326","author":"Campbell","year":"1997","journal-title":"Biochem. J."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"D571","DOI":"10.1093\/nar\/gkab1045","article-title":"The carbohydrate-active enzyme database: Functions and literature","volume":"50","author":"Drula","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"7945","DOI":"10.1073\/pnas.95.14.7945","article-title":"Activity of the yeast MNN1 \u03b1-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases","volume":"95","author":"Wiggins","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s00018-015-2066-0","article-title":"Glycosyltransferase complexes in eukaryotes: Long-known, prevalent but still unrecognized","volume":"73","author":"Kellokumpu","year":"2016","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Grewal, R.K., Shaikh, A.R., Gorle, S., Kaur, M., Videira, P.A., Cavallo, L., and Chawla, M. (2021). Structural insights in mammalian sialyltransferases and fucosyltransferases: We have come a long way, but it is still a long way down. Molecules, 26.","DOI":"10.3390\/molecules26175203"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1042\/BCJ20200505","article-title":"NDP-rhamnose biosynthesis and rhamnosyltransferases: Building diverse glycoconjugates in nature","volume":"478","author":"Wagstaff","year":"2021","journal-title":"Biochem. J."}],"container-title":["Journal of Fungi"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2309-608X\/8\/5\/529\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:15:27Z","timestamp":1760138127000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2309-608X\/8\/5\/529"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,5,20]]},"references-count":65,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["jof8050529"],"URL":"https:\/\/doi.org\/10.3390\/jof8050529","relation":{},"ISSN":["2309-608X"],"issn-type":[{"value":"2309-608X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,5,20]]}}}