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The ectodomain of rabies virus glycoprotein determines dendritic cell activation.

Abstract：

:The immune evasion of wild-type (wt) rabies virus (RABV) has been attributed to its glycoprotein (G), particularly to their inefficiency to bind/enter into dendritic cells (DCs). However, the domain responsible for G-mediated DC activation is not clear. In the present study, attempts were made to map the domain(s) on the G involved in differential DC activation using laboratory-adapted and wt viruses. Recombinant RABVs with exchange in each of the structural domains such as signal peptide (sp), ectodomain (et), transmembrane domain (tm), cytoplasmic tail (ct) of the G between wt and laboratory-adapted strains were constructed. Characterizations of these recombinant RABVs show that the viruses containing the sp, tm and ct from the wt G are capable of growing in high titer by efficient cell-to-cell spread, similar to laboratory-adapted virus. On the other hand, recombinant virus containing the et domain from wt G was inefficient in cell-to-cell spread and grew in lower levels, similar to the wt RABV. Analysis of DC activation shows that viruses containing sp and tm from wt G are efficient in binding to and activating DCs. However, viruses containing the et domain from wt G are incompetent in binding to and activating DCs. Analysis of the G expression in the infected cells suggests that the level of G expression is regulated solely by the ct domain, indicating the level of G expression and DC activation are governed by different domains. Together, our results demonstrate that G-mediated DC activation is regulated by the et domain while the level of G expression by the ct domain.

journal_name

Antiviral Res

journal_title

Antiviral research

authors

Huang J,Zhang Y,Huang Y,Gnanadurai CW,Zhou M,Zhao L,Fu ZF

doi

10.1016/j.antiviral.2017.01.022

subject

Has Abstract

pub_date

2017-05-01 00:00:00

pages

1-6

eissn

0166-3542

issn

1872-9096

pii

S0166-3542(16)30448-X

journal_volume

141

pub_type

杂志文章

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