Literature DB >> 11689673

An N-terminal domain of herpes simplex virus type Ig E is capable of forming stable complexes with gI.

S M Rizvi1, M Raghavan.   

Abstract

Using limited proteolytic analyses, we show that gE present in soluble herpes simplex virus type 1 gE-gI complexes is cleaved into a C-terminal (CgE) and an N-terminal (NgE) domain. The domain boundary is in the vicinity of residue 188 of mature gE. NgE, but not CgE, forms a stable complex with soluble gI.

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Year:  2001        PMID: 11689673      PMCID: PMC114778          DOI: 10.1128/JVI.75.23.11897-11901.2001

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  18 in total

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4.  Herpes simplex virus IgG Fc receptors induced using recombinant adenovirus vectors expressing glycoproteins E and I.

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4.  Induction of Rod-Shaped Structures by Herpes Simplex Virus Glycoprotein I.

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8.  The amino terminus of varicella-zoster virus (VZV) glycoprotein E is required for binding to insulin-degrading enzyme, a VZV receptor.

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9.  Immunization strategies to block the herpes simplex virus type 1 immunoglobulin G Fc receptor.

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