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Journal of Virology, October 2009, p. 10299-10304, Vol. 83, No. 19
0022-538X/09/$08.00+0     doi:10.1128/JVI.00217-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mapping of Functional Domains in Herpesvirus Saimiri Complement Control Protein Homolog: Complement Control Protein Domain 2 Is the Smallest Structural Unit Displaying Cofactor and Decay-Accelerating Activities{triangledown}

Akhilesh K. Singh,{dagger} Viveka Nand Yadav, Kalyani Pyaram, Jayati Mullick, and Arvind Sahu*

National Centre for Cell Science, Pune University Campus, Ganeshkhind, Pune 411007, India

Received 30 January 2009/ Accepted 17 July 2009

Herpesvirus saimiri encodes a functional homolog of human regulator-of-complement-activation proteins named CCPH that inactivates complement by accelerating the decay of C3 convertases and by serving as a cofactor in factor I-mediated inactivation of their subunits C3b and C4b. Here, we map the functional domains of CCPH. We demonstrate that short consensus repeat 2 (SCR2) is the minimum domain essential for classical/lectin pathway C3 convertase decay-accelerating activity as well as for factor I cofactor activity for C3b and C4b. Thus, CCPH is the first example wherein a single SCR domain has been shown to display complement regulatory functions.

* Corresponding author. Mailing address: National Centre for Cell Science, Pune University Campus, Ganeshkhind, Pune 411007, India. Phone: 91-20-2570-8083. Fax: 91-20-2569-2259. E-mail: arvindsahu{at}nccs.res.in

{triangledown} Published ahead of print on 29 July 2009.

{dagger} Present address: Department of Molecular Biophysics and Biochemistry, School of Medicine, Yale University, New Haven, CT 06520.

Journal of Virology, October 2009, p. 10299-10304, Vol. 83, No. 19
0022-538X/09/$08.00+0     doi:10.1128/JVI.00217-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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