Respiratory syncytial virus (RSV) is an important cause of lower respiratory tract disease, particularly prevalent in children, and for which there is no efficient vaccine currently available. In addition the viral and host mechanisms that modulate the immune response and disease pathogenesis remain unknown. In August Nature Immunology Ralph Tripp and colleagues from the National Centers for Infectious Diseases, Atlanta, show that a RSV surface protein, the G glycoprotein, has structural and functional features that are similar to the leukocyte chemoattractant Fkn: it seems that the virus uses this protein to facilitate infection and modify immune response.

Using CX3CR1-transfected human embryonic kidney cells Tripp et al. found that the RSV G glycoprotein binds to the CX3CR1 receptor — a receptor specific for the CX3C chemokine fractalkine and subsequent induction of leukocyte chemotaxis. In addition, G glycoprotein binding through the CX3C receptor appeared to facilitate the viral infection (Nat...

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