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Secreted poxvirus chemokine binding proteins
1Department of Biochemistry, University of Alberta, Edmonton, Canada.
Journal of Leukocyte Biology
|November 19, 1997
Summary
Myxoma virus uses two secreted proteins, chemokine binding protein-I (CBP-I) and CBP-II, to bind and neutralize host chemokines. This viral strategy prevents inflammatory cell migration to infection sites, aiding viral evasion.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Poxviruses possess immunomodulatory proteins that disrupt host cytokine networks.
- Myxoma virus, a rabbit pathogen, secretes two glycoproteins that bind chemokines.
Purpose of the Study:
- To characterize two myxoma virus secreted proteins, M-T7 (CBP-I) and M-T1 (CBP-II), and their role in chemokine binding.
- To investigate the impact of CBP-I and CBP-II on leukocyte trafficking during viral infections.
Main Methods:
- Purification and binding studies of M-T7 protein.
- Analysis of recombinant poxviruses with deleted CBP-I or CBP-II genes.
- Assessment of leukocyte infiltration into virus-infected lesions.
Main Results:
- M-T7 (CBP-I) binds multiple chemokine families (CXC, CC, C) via conserved heparin-binding domains.
- M-T1 (CBP-II) is a member of a larger poxviral protein superfamily.
- Deletion of CBP-I or CBP-II genes significantly altered leukocyte trafficking to infected tissues.
Conclusions:
- CBP-I and CBP-II represent novel secreted viral proteins that bind multiple chemokine families.
- These viral proteins likely function to prevent early inflammatory cell migration into virus-infected tissues.
- The interaction with chemokine heparin-binding domains is a potential mechanism for altering chemokine functions in vivo.