当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > The herpes simplex virus-1 glycoprotein E (gE) mediates IgG binding and cell-to-cell spread through distinct gE domains.

The herpes simplex virus-1 glycoprotein E (gE) mediates IgG binding and cell-to-cell spread through distinct gE domains.

Abstract：

:Herpes simplex virus-1 (HSV-1) glycoprotein E (gE) is a multifunctional protein capable of both binding the Fc portion of IgG and mediating cell-to-cell spread of HSV-1. Here we report that the domain on gE involved in IgG binding is distinct from the domain involved in mediating cell-to-cell spread. To do this we have used five mutants of the HSV-1 strain NS: NS-gE(null), a gE deletion virus; rNS-gE(null), a gE rescued virus; NS-gE339, a gE mutant virus with a four amino acid insert at position 339; rNS-gE339, a gE rescue of NS-gE339; and NS-gE406, a gE mutant virus with the same four amino acids inserted at position 406. Using IgG coated sheep red blood cells in rosetting assays, we show that the NS-gE339 does not bind IgG, yet retains the ability to mediate normal cell-to-cell spread. These results demonstrate that the gE domain involved in IgG binding differs from the domain involved in cell-to-cell spread.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Weeks BS,Sundaresan P,Nagashunmugam T,Kang E,Friedman HM

doi

10.1006/bbrc.1997.6720

subject

Has Abstract

pub_date

1997-06-09 00:00:00

pages

31-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)96720-6

journal_volume

235

pub_type

杂志文章

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