Abstract:
:Most poxviruses, including variola, the causative agent of smallpox, express a secreted protein of 35 kDa, vCCI, which binds CC-chemokines with high affinity. This viral protein competes with the host cellular CC-chemokine receptors (CCRs), reducing inflammation and interfering with the host immune response. Such proteins or derivatives may have therapeutic uses as anti-inflammatory agents. We have determined the crystal structure to 1.85-A resolution of vCCI from cowpox virus, the prototype of this poxvirus virulence factor. The molecule is a beta-sandwich of topology not previously described. A patch of conserved residues on the exposed face of a beta-sheet that is strongly negatively charged might have a role in binding of CC-chemokines, which are positively charged.
journal_name
Proc Natl Acad Sci U S Aauthors
Carfí A,Smith CA,Smolak PJ,McGrew J,Wiley DCdoi
10.1073/pnas.96.22.12379keywords:
subject
Has Abstractpub_date
1999-10-26 00:00:00pages
12379-83issue
22eissn
0027-8424issn
1091-6490journal_volume
96pub_type
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