Characterization of modified hepatitis C virus E2 proteins expressed on the cell surface.

Abstract:

:The envelope proteins of hepatitis C virus (HCV) are the likely targets of neutralizing antibodies and their molecular and functional characterization is relevant for vaccine development. We previously showed that surface-expressed E2 is a better immunogen than intracellular E2 and, therefore, we were interested in exploring more efficient ways to present E2 protein on the cell surface. We found that E2 targeted to the cell surface by replacement of its transmembrane domain did not bring E1 to the surface although E1 could be expressed independently on the cell surface if its transmembrane domain was similarly replaced. FACS analysis suggested that E2 expressed on the cell surface acquired its native conformation more efficiently when truncated at aa 661 than when truncated at aa 715. The shorter form of truncated E2 better retained the ability to bind the second extracellular loop (EC2) of CD81, the putative HCV receptor. Interestingly, deletion of the hypervariable region 1 (HVR1) did not perceptibly alter E2 structure; cell-surface forms of E2 lacking the HVR1 remained reactive with conformation-sensitive MAbs and were able to bind recombinant EC2 of CD81.

journal_name

Virology

journal_title

Virology

authors

Forns X,Allander T,Rohwer-Nutter P,Bukh J

doi

10.1006/viro.2000.0419

subject

Has Abstract

pub_date

2000-08-15 00:00:00

pages

75-85

issue

1

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(00)90419-7

journal_volume

274

pub_type

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