Regular Article
Respiratory Syncytial Virus—Viral Biology and the Host Response

https://doi.org/10.1053/jinf.2002.1015Get rights and content

Abstract

Respiratory syncytial virus (RSV) is the most important cause of respiratory tract infection in infants. We have an incomplete understanding of the reasons why some infants are more severely affected by RSV than others. There is no effective antiviral treatment for the infection. Advances in our understanding of the biology of RSV, particularly in relation to the attachment protein G and the fusion protein F, have revealed potential targets for new antiviral therapies and vaccine development. In response to RSV infection an intense inflammatory response is triggered, mediated initially by the infected airway epithelial cells. Cell mediated responses are important in controlling the extent of infection and in viral clearance. Humoral responses are important in protection. There is early evidence that genetic variation of the host response can influence the outcome of RSV-induced bronchiolitis.

References (55)

  • J Schlender et al.

    Bovine respiratory syncytial virus nonstructural proteins NS1 and NS2 cooperatively antagonize α/β interferon-induced antiviral response

    J Virol

    (2000)
  • S Levine et al.

    Demonstration that glycoprotein G is the attachment protein of respiratory syncitial virus

    J Gen Virol

    (1987)
  • PA Cane

    Molecular epidemiology of respiratory syncytial virus

    Rev Med Virol

    (2001)
  • PA Cane

    Analysis of linear epitopes recognized by the primary human antibody response to variable region of the attachment (G) protein of respiratory syncytial virus

    J Med Virol

    (1997)
  • RA Karron et al.

    Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: Clinical evaluation and molecular characterization of a cold passaged, attenuated RSV subgroup B mutant

    Proc Natl Acad Sci USA

    (1997)
  • MN Teng et al.

    Identification of the respiratory syncytial virus proteins required for formation and passage of helper-dependent infectious particles

    J Virol

    (1998)
  • SA Feldman et al.

    Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G

    J Virol

    (1999)
  • PR Johnson et al.

    The G glycoprotein of human respiratory syncytial virus of subgroups A and B: extensive sequence divergence between antigenically related proteins

    Proc Natl Acad Sci USA

    (1987)
  • RA Tripp et al.

    CX3C chemokine mimicry by respiratory syncytial virus G glycoprotein

    Nature Immunol

    (2001)
  • Collins, PL, McIntosh, K, Chanock, RM, et al., Respiratory syncytial virus, Fields, BNKnipe, DMHowley, PM, et al.,...
  • PL Collins et al.

    Post-translational processing and oligomerization of the fusion glycoprotein of human respiratory syncytial virus

    J Gen Virol

    (1991)
  • DM Lambert et al.

    Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion

    Proc Natl Acad Sci USA

    (1996)
  • MK Pastey et al.

    RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation

    J Virol

    (1999)
  • MK Pastey et al.

    A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3

    Nat Med

    (2000)
  • TL Gower et al.

    Antiviral activity of lovastatin against respiratory syncytial virus in vivo and in vitro

    Antimicrob Agents Chemother

    (2001)
  • W Aherne et al.

    Pathological changes in virus infections of the lower respiratory tract in children

    J Clin Pathol

    (1970)
  • ML Everard et al.

    Analysis of cells obtained by bronchial lavage of infants with respiratory syncytial virus infection

    Arch Dis Child

    (1994)
  • Cited by (0)

    f1

    Please address all correspondence to: Doug Hacking, MRC Clinical Research Training Fellow. Tel.: +441865221061; Fax: +441865220479; E-mail address:[email protected] (D. Hacking).

    View full text