Abstract

Poxviruses and herpesviruses encode a unique family of proteins that are secreted from infected cells and bind chemokines, in spite of their lack of amino acid sequence similarity to cellular chemokine receptors. Many of the methods used with host chemokines and chemokine receptors may be used to characterize these virus-encoded chemokine inhibitors. Here we focus on methodologies that have been adapted to identify secreted chemokine binding proteins from viruses, to determine their binding specificity for chemokines and to characterize their interaction with the chemokine domains involved in the recognition of chemokine receptors or glycosaminoglycans.

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