Parallel Evolution of Chemokine Binding by Structurally Related Herpesvirus Decoy Receptors

Lubman, Olga Y.; Fremont, Daved H.

doi:10.1016/j.str.2015.10.018

Title: Parallel Evolution of Chemokine Binding by Structurally Related Herpesvirus Decoy Receptors

Journal Article · 03 December 2015 · Structure

DOI: https://doi.org/10.1016/j.str.2015.10.018 · OSTI ID:1237760

Lubman, Olga Y. ^[1]; Fremont, Daved H. ^[1]

Washington Univ. School of Medicine, St. Louis, MO (United States)

A wide variety of pathogens targets chemokine signaling networks in order to disrupt host immune surveillance and defense. Here, we report a structural and mutational analysis of rodent herpesvirus Peru encoded R17, a potent chemokine inhibitor that sequesters CC and C chemokines with high affinity. R17 consists of a pair of β-sandwich domains linked together by a bridging sheet, which form an acidic binding cleft for the chemokine CCL3 on the opposite face of a basic surface cluster that binds glycosaminoglycans. R17 promiscuously engages chemokines primarily through the same N-loop determinants used for host receptor recognition while residues located in the chemokine 40s loop drive kinetically stable complex formation. Here, the core fold adopted by R17 is unexpectedly similar to that of the M3 chemokine decoy receptor encoded by MHV-68, although, strikingly, neither the location of ligand engagement nor the stoichiometry of binding is conserved, suggesting that their functions evolved independently.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: NIAID

Grant/Contract Number:: R01 AI019687; U54 AI057160

OSTI ID:: 1237760

Journal Information:: Structure, Vol. 24, Issue 1; ISSN 0969-2126

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 15 works

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