Author: Irie Takashi Liu Yuliang Drolet Barbara S. Carnero Elena García-Sastre Adolfo Harty Ronald N.
Publisher: MDPI
E-ISSN: 1999-4915|4|9|1605-1618
ISSN: 1999-4915
Source: Viruses, Vol.4, Iss.9, 2012-09, pp. : 1605-1618
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Abstract
Vesicular stomatitis virus (VSV) is an important vector-borne pathogen of bovine and equine species, causing a reportable vesicular disease. The matrix (M) protein of VSV is multifunctional and plays a key role in cytopathogenesis, apoptosis, host protein shut-off, and virion assembly/budding. Our previous findings indicated that mutations of residues flanking the 37PSAP40 motif within the M protein resulted in VSV recombinants having attenuated phenotypes in mice. In this report, we characterize the phenotype of VSV recombinant PS > A4 (which harbors four alanines (AAAA) in place of the PSAP motif without disruption of flanking residues) in both mice, and in
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