{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T17:10:01Z","timestamp":1788801001513,"version":"build-2803163510"},"reference-count":54,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T00:00:00Z","timestamp":1788739200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004763","name":"Inner Mongolia Natural Science Foundation","doi-asserted-by":"publisher","award":["2026QC0675"],"award-info":[{"award-number":["2026QC0675"]}],"id":[{"id":"10.13039\/501100004763","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100017534","name":"Introducing Talents Scientific Research Project of Inner Mongolia Medical University","doi-asserted-by":"publisher","award":["DC2300001919"],"award-info":[{"award-number":["DC2300001919"]}],"id":[{"id":"10.13039\/100017534","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011811","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["RZ2200002645"],"award-info":[{"award-number":["RZ2200002645"]}],"id":[{"id":"10.13039\/501100011811","id-type":"DOI","asserted-by":"publisher"}]},{"award":["RZ2200002645"],"award-info":[{"award-number":["RZ2200002645"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"publisher"}]},{"name":"Key Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, the Ministry of Agriculture"},{"name":"Ruminant Animal Disease Diagnosis Center, Inner Mongolia Agricultural University"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Vet. Sci.","Veterinary Sciences"],"abstract":"<jats:p>Rabies virus causes fatal neurological disease, but the mechanisms by which its glycoprotein G influences neuronal dysfunction remain incompletely understood. In this study, we rescued two recombinant RABV LBNSE strains carrying G proteins from either the attenuated SAD-B19 strain or the virulent CVS11 strain, designated as rLBNSE-SfG and rLBNSE-CfG, respectively. Infection of primary mouse neurons and challenge experiments in mice showed that rLBNSE-CfG was associated with increased early neuronal infectivity and greater neurovirulence after intracerebral (i.c.) injection. Western blot analysis revealed that the SAD-B19-derived G protein exhibited a higher apparent molecular weight than the CVS11-derived G protein. Bioinformatic analysis identified strain-specific differences in putative post-translational modification sites, which may contribute to the observed migration difference. Quantitative proteomic analysis of mouse brain tissue showed that proteins downregulated in the rLBNSE-CfG group were enriched in synaptic vesicle cycle-related pathways and synapse-associated Gene Ontology (GO) terms. Integrated analysis identified a SNARE-associated module containing Snap25, Stx1a, and Vamp2, among which Vamp2 was significantly reduced in the rLBNSE-CfG group. In primary neurons, reduced Vamp2 abundance was associated with the extracellular domain of CVS11 G protein. These findings associate CVS11-derived G protein variation with reduced Vamp2 abundance and a presynaptic vesicle-related proteomic signature, although whether these molecular alterations directly impair synaptic vesicle release remains to be determined.<\/jats:p>","DOI":"10.3390\/vetsci13090919","type":"journal-article","created":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T16:30:02Z","timestamp":1788798602000},"page":"919","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Rabies Virus Glycoprotein G Variation Is Associated with Neurovirulence and Reduced Vamp2 Abundance in a Mouse Model of Direct CNS Infection"],"prefix":"10.3390","volume":"13","author":[{"given":"Chunyu","family":"Liu","sequence":"first","affiliation":[{"name":"College of Basic Medicine, Inner Mongolia Medical University, Hohhot 010110, China"},{"name":"College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot 010018, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-original-draft","vocabulary":"credit"},{"role":"conceptualization","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5023-3270","authenticated-orcid":false,"given":"Hao","family":"Guo","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Inner Mongolia University, Hohhot 010020, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-original-draft","vocabulary":"credit"},{"role":"validation","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Kun","family":"Yin","sequence":"additional","affiliation":[{"name":"Zhoukou Academy of Agricultural Sciences, Zhoukou 466001, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"conceptualization","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"}]},{"given":"Yuming","family":"Sun","sequence":"additional","affiliation":[{"name":"Yulin Animal Husbandry and Veterinary Service Center, Yulin 719000, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"investigation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"}]},{"given":"Zipeng","family":"Ma","sequence":"additional","affiliation":[{"name":"Yulin Animal Husbandry Comprehensive Service Station, Yulin 719000, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"investigation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"}]},{"given":"Fengxue","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot 010018, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"resources","vocabulary":"credit"},{"role":"validation","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-5154-2607","authenticated-orcid":false,"given":"Yan","family":"Niu","sequence":"additional","affiliation":[{"name":"College of Basic Medicine, Inner Mongolia Medical University, Hohhot 010110, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"conceptualization","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Yongjun","family":"Wen","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot 010018, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"conceptualization","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"231","DOI":"10.7589\/0090-3558-36.2.231","article-title":"Bat rabies in urban centers in Chile","volume":"36","author":"Favi","year":"2000","journal-title":"J. Wildl. Dis."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/S0140-6736(04)15792-9","article-title":"Rabies and other lyssavirus diseases","volume":"363","author":"Warrell","year":"2004","journal-title":"Lancet"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"S20","DOI":"10.1016\/S0264-410X(96)00312-X","article-title":"Rabies and rabies research: Past, present and future","volume":"15","author":"Fu","year":"1997","journal-title":"Vaccine"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.micpath.2011.10.001","article-title":"Changes in microRNA expression induced by rabies virus infection in mouse brains","volume":"52","author":"Zhao","year":"2012","journal-title":"Microb. Pathog."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/0042-6822(92)90465-2","article-title":"Rabies virus glycoprotein is a trimer","volume":"187","author":"Gaudin","year":"1992","journal-title":"Virology"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Cai, X., Zhou, K., Alvarez-Cabrera, A.L., Si, Z., Wang, H., He, Y., Li, C., and Zhou, Z.H. (2024). Structural Heterogeneity of the Rabies Virus Virion. Viruses, 16.","DOI":"10.3390\/v16091447"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.pep.2008.02.014","article-title":"Expression, purification and immunodetection of a recombinant fragment (residues 179\u2013281) of the G protein from rabies virus ERA strain","volume":"59","author":"Bassi","year":"2008","journal-title":"Protein Expr. Purif."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"9639","DOI":"10.1038\/s41598-019-46126-7","article-title":"Cryo EM structure of the rabies virus ribonucleoprotein complex","volume":"9","author":"Riedel","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_9","first-page":"45","article-title":"Pathogenesis of rabies","volume":"292","author":"Dietzschold","year":"2005","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.virusres.2012.12.011","article-title":"Pathobiology of rabies virus and the European bat lyssaviruses in experimentally infected mice","volume":"172","author":"Healy","year":"2013","journal-title":"Virus Res."},{"key":"ref_11","first-page":"S14","article-title":"Rabies virus glycoprotein: Structure, immunogenicity and pathogenic role","volume":"25","author":"Ross","year":"2008","journal-title":"Rev. Chil. Infectol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1093\/glycob\/cwi046","article-title":"N-glycosylation at one rabies virus glycoprotein sequon influences N-glycan processing at a distant sequon on the same molecule","volume":"15","author":"Wojczyk","year":"2005","journal-title":"Glycobiology"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Li, C., Zhang, H., Ji, L., Wang, X., Wen, Y., Li, G., Fu, Z.F., and Yang, Y. (2019). Deficient Incorporation of Rabies Virus Glycoprotein into Virions Enhances Virus-Induced Immune Evasion and Viral Pathogenicity. Viruses, 11.","DOI":"10.3390\/v11030218"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1222","DOI":"10.1099\/jgv.0.001299","article-title":"Codon optimization of G protein enhances rabies virus-induced humoral immunity","volume":"100","author":"Pei","year":"2019","journal-title":"J. Gen. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/j.1348-0421.2009.00192.x","article-title":"Amino acid substitutions at positions 242, 255 and 268 in rabies virus glycoprotein affect spread of viral infection","volume":"54","author":"Ito","year":"2010","journal-title":"Microbiol. Immunol."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Li, C., Wang, Y., Liu, H., Zhang, X., Baolige, D., Zhao, S., Hu, W., and Yang, Y. (2021). Change in the Single Amino Acid Site 83 in Rabies Virus Glycoprotein Enhances the BBB Permeability and Reduces Viral Pathogenicity. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.632957"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"9650","DOI":"10.1096\/fj.201902577R","article-title":"Single amino acid change at position 255 in rabies virus glycoprotein decreases viral pathogenicity","volume":"34","author":"Luo","year":"2020","journal-title":"FASEB J."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Luo, J., Zhang, B., Wu, Y., and Guo, X. (2020). Amino Acid Mutation in Position 349 of Glycoprotein Affect the Pathogenicity of Rabies Virus. Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.00481"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.virusres.2013.10.015","article-title":"Efficient N-glycosylation at position 37, but not at position 146, in the street rabies virus glycoprotein reduces pathogenicity","volume":"179","author":"Yamada","year":"2014","journal-title":"Virus Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s00705-013-1805-5","article-title":"Characterization of street rabies virus variants with an additional N-glycan at position 247 in the glycoprotein","volume":"159","author":"Yamada","year":"2014","journal-title":"Arch. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"001935","DOI":"10.1099\/jgv.0.001935","article-title":"Internalization of rabies virus glycoprotein differs between pathogenic and attenuated virus strains","volume":"104","author":"Almasoud","year":"2023","journal-title":"J. Gen. Virol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1016\/j.celrep.2016.03.067","article-title":"Improved Monosynaptic Neural Circuit Tracing Using Engineered Rabies Virus Glycoproteins","volume":"15","author":"Kim","year":"2016","journal-title":"Cell Rep."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"373","DOI":"10.3109\/13550280009018301","article-title":"Reinvestigation of the role of the rabies virus glycoprotein in viral pathogenesis using a reverse genetics approach","volume":"6","author":"Morimoto","year":"2000","journal-title":"J. Neurovirol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1016\/j.neuron.2016.01.004","article-title":"Rabies Virus CVS-N2c(\u0394G) Strain Enhances Retrograde Synaptic Transfer and Neuronal Viability","volume":"89","author":"Reardon","year":"2016","journal-title":"Neuron"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1080\/13550280500385310","article-title":"Glycoprotein-mediated induction of apoptosis limits the spread of attenuated rabies viruses in the central nervous system of mice","volume":"11","author":"Sarmento","year":"2005","journal-title":"J. Neurovirol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1136\/vr.131.3.55","article-title":"Pathogenicity of SAD rabies vaccine given orally in chacma baboons (Papio ursinus)","volume":"131","author":"Bingham","year":"1992","journal-title":"Vet. Rec."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1046\/j.1439-0450.2001.00440.x","article-title":"Immunogenicity and efficacy of the oral rabies vaccine SAD B19 in foxes","volume":"48","author":"Neubert","year":"2001","journal-title":"J. Vet. Med. B Infect. Dis. Vet. Public Health"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"548","DOI":"10.7589\/0090-3558-25.4.548","article-title":"Oral vaccination of raccoons (Procyon lotor) with an attenuated (SAD-B19) rabies virus vaccine","volume":"25","author":"Rupprecht","year":"1989","journal-title":"J. Wildl. Dis."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.2460\/javma.1982.180.11.1336","article-title":"Vaccine-induced rabies in four cats","volume":"180","author":"Esh","year":"1982","journal-title":"J. Am. Vet. Med. Assoc."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1093\/oxfordjournals.aje.a112302","article-title":"Oral rabies vaccine: Evaluation of its infectivity in three species of rodents","volume":"104","author":"Winkler","year":"1976","journal-title":"Am. J. Epidemiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0264-410X(94)90095-7","article-title":"Vaccination against rabies: Construction and characterization of SAG2, a double avirulent derivative of SADBern","volume":"12","author":"Lafay","year":"1994","journal-title":"Vaccine"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"420","DOI":"10.7589\/0090-3558-38.2.420","article-title":"Oral efficacy of an attenuated rabies virus vaccine in skunks and raccoons","volume":"38","author":"Hanlon","year":"2002","journal-title":"J. Wildl. Dis."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1128\/JVI.01552-10","article-title":"Rabies virus expressing dendritic cell-activating molecules enhances the innate and adaptive immune response to vaccination","volume":"85","author":"Wen","year":"2011","journal-title":"J. Virol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1007\/s00401-005-0006-z","article-title":"Comparative pathogenesis of recombinant rabies vaccine strain SAD-L16 and SAD-D29 with replacement of Arg333 in the glycoprotein after peripheral inoculation of neonatal mice: Less neurovirulent strain is a stronger inducer of neuronal apoptosis","volume":"111","author":"Jackson","year":"2006","journal-title":"Acta Neuropathol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"14141","DOI":"10.1128\/JVI.79.22.14141-14148.2005","article-title":"A single amino acid change in rabies virus glycoprotein increases virus spread and enhances virus pathogenicity","volume":"79","author":"Faber","year":"2005","journal-title":"J. Virol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"4195","DOI":"10.1002\/j.1460-2075.1994.tb06739.x","article-title":"Infectious rabies viruses from cloned cDNA","volume":"13","author":"Schnell","year":"1994","journal-title":"EMBO J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0166-0934(02)00249-5","article-title":"An improved method for recovering rabies virus from cloned cDNA","volume":"107","author":"Inoue","year":"2003","journal-title":"J. Virol. Methods"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"108699","DOI":"10.1016\/j.vetmic.2020.108699","article-title":"Snap25 regulates the release of the Rabies virus in nerve cells via SNARE complex-mediated membrane fusion","volume":"245","author":"Yin","year":"2020","journal-title":"Vet. Microbiol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s11262-013-0952-9","article-title":"A reassessment of the evolutionary timescale of bat rabies viruses based upon glycoprotein gene sequences","volume":"47","author":"Kuzmina","year":"2013","journal-title":"Virus Genes"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"387","DOI":"10.7883\/yoken.JJID.2014.533","article-title":"Association between RABV G Proteins Transported from the Perinuclear Space to the Cell Surface Membrane and N-Glycosylation of the Sequon Asn(204)","volume":"68","author":"Hamamoto","year":"2015","journal-title":"Jpn. J. Infect. Dis."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"108552","DOI":"10.1016\/j.vetmic.2019.108552","article-title":"Comprehensive analysis of the ubiquitome in rabies virus-infected brain tissue of Mus musculus","volume":"241","author":"Cai","year":"2020","journal-title":"Vet. Microbiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.virusres.2006.01.014","article-title":"A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein","volume":"119","author":"Inoue","year":"2006","journal-title":"Virus Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"12559","DOI":"10.1038\/s41598-024-63337-9","article-title":"Construction of Vero cell-adapted rabies vaccine strain by five amino acid substitutions in HEP-Flury strain","volume":"14","author":"Harada","year":"2024","journal-title":"Sci. Rep."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1146\/annurev.neuro.26.041002.131412","article-title":"The synaptic vesicle cycle","volume":"27","author":"Sudhof","year":"2004","journal-title":"Annu. Rev. Neurosci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/nrm2002","article-title":"SNAREs\u2014engines for membrane fusion","volume":"7","author":"Jahn","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1126\/science.1064335","article-title":"SNARE function analyzed in synaptobrevin\/VAMP knockout mice","volume":"294","author":"Schoch","year":"2001","journal-title":"Science"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1186\/s13195-021-00861-0","article-title":"VAMP-2 is a surrogate cerebrospinal fluid marker of Alzheimer-related cognitive impairment in adults with Down syndrome","volume":"13","author":"Lleo","year":"2021","journal-title":"Alzheimer\u2019s Res. Ther."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1186\/s13195-023-01336-0","article-title":"Evaluation of cerebrospinal fluid levels of synaptic vesicle protein, VAMP-2, across the sporadic Alzheimer\u2019s disease continuum","volume":"15","author":"Goossens","year":"2023","journal-title":"Alzheimers Res. Ther."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"5647","DOI":"10.1242\/jcs.02658","article-title":"SV2A and SV2C are not vesicular Ca2+ transporters but control glucose-evoked granule recruitment","volume":"118","author":"Iezzi","year":"2005","journal-title":"J. Cell Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1152\/physrev.2000.80.2.717","article-title":"Neurotoxins affecting neuroexocytosis","volume":"80","author":"Schiavo","year":"2000","journal-title":"Physiol. Rev."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1038\/s41593-026-02254-8","article-title":"HSV-1 strain H129 co-opts neuronal synaptic transmission machinery for its transsynaptic spread","volume":"29","author":"Qin","year":"2026","journal-title":"Nat. Neurosci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"e62273","DOI":"10.7554\/eLife.62273","article-title":"Virus infection of the CNS disrupts the immune-neural-synaptic axis via induction of pleiotropic gene regulation of host responses","volume":"10","author":"Maximova","year":"2021","journal-title":"eLife"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1126\/science.7053569","article-title":"Is the acetylcholine receptor a rabies virus receptor?","volume":"215","author":"Lentz","year":"1982","journal-title":"Science"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"7181","DOI":"10.1128\/JVI.72.9.7181-7190.1998","article-title":"The neural cell adhesion molecule is a receptor for rabies virus","volume":"72","author":"Thoulouze","year":"1998","journal-title":"J. Virol."}],"container-title":["Veterinary Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2306-7381\/13\/9\/919\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T16:54:38Z","timestamp":1788800078000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2306-7381\/13\/9\/919"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,7]]},"references-count":54,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2026,9]]}},"alternative-id":["vetsci13090919"],"URL":"https:\/\/doi.org\/10.3390\/vetsci13090919","relation":{},"ISSN":["2306-7381"],"issn-type":[{"value":"2306-7381","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,7]]}}}