The trypsin-sensitive RVER domain in the capsid proteins of minute virus of mice is required for efficient cell binding and viral infection but not for proteolytic processing in vivo.
Analysis of a series of mutations in the trypsin-sensitive RVER region of the amino terminal domain in the capsid proteins (VP1 and VP2) of the autonomous parvovirus, minute virus of mice (MVM), demonstrates that this sequence is not essential for proteolytic processing of VP2 into VP3 in vivo, but specific amino acids within this domain are important for viral infection. Analysis of the most deficient of these mutants, VP(delta 2842-2863), a 7-aa deletion of aa 159-165 in VP1 and 17-23 in VP2, has identified at least two steps in MVM infection in which this domain is important. VP(delta 2842-2863) was 3-fold defective in binding to murine A9(2L) cells and, when an equivalent amount of virus was bound to cells, additionally 10-fold deficient compared to wild-type in initiating a productive infection. However, in those cells effectively infected, VP(delta 2843-2863) replicated similar to wild-type. These results suggest that these seven amino acids constitute a region important for both binding and a subsequent step prior to the start of DNA replication such as viral uptake or transport to the nucleus.
Tullis
G E
GE
Department of Molecular Microbiology and Immunology, University of Missouri, Columbia School of Medicine 65212.
Burger
L R
LR
Pintel
D J
DJ
D000595:Amino Acid Sequence; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D036022:Capsid Proteins; D002478:Cells, Cultured; D004252:DNA Mutational Analysis; D008915:Minute Virus of Mice / Q000737:chemistry* / Q000472:pathogenicity; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011499:Protein Processing, Post-Translational; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000494:pharmacology; D014774:Virulence
D036022:Capsid Proteins; C442549:VP1 protein, Mice minute virus; D014357:Trypsin