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Article

Effect of polylysine on the early stages of infection of wild type pseudorabies virus and of mutants defective in gIII.

Virology - 1 Nov 1990

Zsak L, Mettenleiter T C, Sugg N, Ben-Porat T

Abstract excerpt

The main pathway of adsorption of pseudorabies virus (PrV) to its host cells is via interactions between viral glycoprotein gIII and a cellular heparin-like receptor. Mutants of PrV deficient in glycoprotein gIII adsorb by an alternative, slower pathway. Penetration into the cells of gIII- mutants is also delayed compared to penetration of wild type virus. We show here that polylysine enhances the adsorption of...

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Identifiers

PMID: 2171208
DOI: 10.1016/0042-6822(90)90301-7

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Effect of polylysine on the early stages of infection of wild type pseudorabies virus and of mutants defective in gIII.PMID 2171208Read ↗

The gIII glycoprotein of pseudorabies virus is involved in two distinct steps of virus attachment.Semantic proximity Read ↗

The amino-terminal one-third of pseudorabies virus glycoprotein gIII contains a functional attachment domain, but this domain is not required for the efficient penetration of Vero cells.Semantic proximity Read ↗

Interaction of glycoprotein gIII with a cellular heparinlike substance mediates adsorption of pseudorabies virus.Semantic proximity Read ↗

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Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE.Semantic proximity Read ↗

A mutant of pseudorabies virus with deletion of glycoprotein gIII gene prepared from a Japanese isolate: it fails to agglutinate mouse erythrocytes.Semantic proximity Read ↗

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