Identification of functional domains in kaposica, the complement control protein homolog of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8).

Abstract:

:Recently it has been shown that kaposica, an immune evasion protein of Kaposi's sarcoma-associated herpesvirus, inactivates complement by acting on C3-convertases by accelerating their decay as well as by acting as a cofactor in factor I-mediated inactivation of their subunits C3b and C4b. Here, we have mapped the functional domains of kaposica. We show that SCRs 1 and 2 (SCRs 1-2) and 1-4 are essential for the classical and alternative pathway C3-convertase decay-accelerating activity (DAA), respectively, while the SCRs 2-3 are required for factor I cofactor activity (CFA) for C3b and C4b. SCR 3 and SCRs 1 and 4, however, contribute to optimal classical pathway DAA and C3b CFA, respectively. Binding data show that SCRs 1-4 and SCRs 1-2 are the smallest structural units required for measuring detectable binding to C3b and C4b, respectively. The heparin-binding site maps to SCR 1.

journal_name

J Virol

journal_title

Journal of virology

authors

Mullick J,Singh AK,Panse Y,Yadav V,Bernet J,Sahu A

doi

10.1128/JVI.79.9.5850-5856.2005

subject

Has Abstract

pub_date

2005-05-01 00:00:00

pages

5850-6

issue

9

eissn

0022-538X

issn

1098-5514

pii

79/9/5850

journal_volume

79

pub_type

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