Protein processing map of poliovirus

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Published inJournal of Virology Vol. 49; no. 3; pp. 873 - 880
Main Authors PALLANSCH, M. A, KEW, O. M, SEMLER, B. L, OMILIANOWSKI, D. R, ANDERSON, C. W, WIMMER, E, RUECKERT, R. R
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.03.1984
Subjects
Amino Acid Sequence
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
HeLa Cells
Humans
Microbiology
Models, Chemical
peptide mapping
poliovirus
Poliovirus - metabolism
protein biosynthesis
Protein Processing, Post-Translational
Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains
Trypsin - metabolism
tryptic peptides
Viral Proteins - analysis
Virology
Proteins
Peptide map
Poliovirus 1
Processing
Online AccessGet full text

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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList Five previously unmapped proteins (5a, 7d, 8, 9b, and 10) were located on the proteolytic processing map of the polyprotein. One of the proteins, 9b, appears to be the sister fragment of a cleavage reaction (P3-9 leads to P3-9b + VPg). Two of the other newly mapped proteins, 8 and 10, have been identified as sister fragments of X-related proteins 3b and 5b; thus, P2-3b leads to P2-8 + P2-5b and P2-5b leads to P2-10 + P2-X. The remaining proteins, 5a and 7d, mapped in the 1b protein and appear to result from the cleavages P3-1b leads to P3-5a + P3-6b and P3-4b leads to P3-7d + P3-6b. These assignments account for over 95% of the total polioviral proteins and complete the mapping of the major processing pathways.
Five previously unmapped proteins (5a, 7d, 8, 9b, and 10) were located on the proteolytic processing map of the polyprotein. One of the proteins, 9b, appears to be the sister fragment of a cleavage reaction (P3-9 arrow right P3-9b + VPg). Two of the other newly mapped proteins, 8 and 10, have been identified as sister fragments of X-related proteins 3b and 5b; thus, P2-3b arrow right P2-8 + P2-8 + P2-5b and P2-5b arrow right P2-10 + P2-X. The remaining proteins, 5a and 7d, mapped in the 1b protein and appear to result from the cleavages P3-1b arrow right P3-5a + P3-6b and P3-4b arrow right P3-7d + P3-6b. These assignments account for over 95% of the total polioviral proteins and complete the mapping of the major processing pathways.
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
Author M A Pallansch
R R Rueckert
E Wimmer
B L Semler
D R Omilianowski
O M Kew
C W Anderson
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Keywords Proteins
Peptide map
Poliovirus 1
Processing
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Five previously unmapped proteins (5a, 7d, 8, 9b, and 10) were located on the proteolytic processing map of the polyprotein. One of the proteins, 9b, appears...
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SubjectTerms Amino Acid Sequence
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
HeLa Cells
Humans
Microbiology
Models, Chemical
peptide mapping
poliovirus
Poliovirus - metabolism
protein biosynthesis
Protein Processing, Post-Translational
Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains
Trypsin - metabolism
tryptic peptides
Viral Proteins - analysis
Virology
Title Protein processing map of poliovirus
URI http://jvi.asm.org/content/49/3/873.abstract
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