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© Gail Rozen-Gagnon, Christine Schmitt,
Cells infected with Chikungunya (CHIK) virus.
Publication : The Journal of general virology

The replication defect of pseudorabies virus induced by targeted α-helix distortion in the syntaxin-like bundle of glycoprotein H (V275P) is corrected by an adjacent compensatory mutation (V271A)

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of general virology - 23 Apr 2015

Böhm S, Backovic M, Klupp BG, Rey FA, Mettenleiter TC, Fuchs W

Link to Pubmed [PMID] – 25908778

J. Gen. Virol. 2015 Apr;

Glycoprotein gH is essential for herpesvirus-induced membrane fusion during entry and cell-to-cell spread. Structural analyses of gH homologues revealed a conserved syntaxin-like bundle motif composed of three -helices. Previous studies showed that targeted disruption of any of these helices strongly impaired maturation, cell surface expression, and fusion activity of pseudorabies virus gH, as well as formation and spread of infectious virus. After passaging of one corresponding mutant (pPrV-gH-V275P) these replication defects were widely corrected by an adjacent, spontaneous amino acid substitution (V271A). Although the doubly mutated gH was still non-functional in fusion assays, its targeted reinsertion into the cloned virus genome (pPrV-gH-V275P-V271A) led to 200-fold increased plaque sizes, and 10000-fold higher virus titers, compared to pPrV-gH-V275P. Thus, our results demonstrate that structural requirements for gH function in in vitro assays and virus replication are different, and that minor amounts of mature gH in virions are sufficient for productive replication.

http://www.ncbi.nlm.nih.gov/pubmed/25908778