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Journal of Virology, July 2005, p. 7967-7978, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.7967-7978.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Junctional Adhesion Molecule A Serves as a Receptor for Prototype and Field-Isolate Strains of Mammalian Reovirus

Jacquelyn A. Campbell,1,2 Pierre Schelling,3 J. Denise Wetzel,2,4 Elizabeth M. Johnson,1,2 J. Craig Forrest,1,2 Greame A. R. Wilson,5 Michel Aurrand-Lions,6 Beat A. Imhof,6 Thilo Stehle,3 and Terence S. Dermody1,2,4*

Departments of Microbiology and Immunology,1 Pediatrics,4 Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University School of Medicine, Nashville, Tennessee 37232,2 Amgen Inc., Thousand Oaks, California 91320,5 Department of Pathology, Centre Medical Universitaire, Geneva, Switzerland,6 Laboratory of Developmental Immunology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 021143

Received 6 January 2005/ Accepted 17 March 2005

Reovirus infections are initiated by the binding of viral attachment protein {sigma}1 to receptors on the surface of host cells. The {sigma}1 protein is an elongated fiber comprised of an N-terminal tail that inserts into the virion and a C-terminal head that extends from the virion surface. The prototype reovirus strains type 1 Lang/53 (T1L/53) and type 3 Dearing/55 (T3D/55) use junctional adhesion molecule A (JAM-A) as a receptor. The C-terminal half of the T3D/55 {sigma}1 protein interacts directly with JAM-A, but the determinants of receptor-binding specificity have not been identified. In this study, we investigated whether JAM-A also mediates the attachment of the prototype reovirus strain type 2 Jones/55 (T2J/55) and a panel of field-isolate strains representing each of the three serotypes. Antibodies specific for JAM-A were capable of inhibiting infections of HeLa cells by T1L/53, T2J/55, and T3D/55, demonstrating that strains of all three serotypes use JAM-A as a receptor. To corroborate these findings, we introduced JAM-A or the structurally related JAM family members JAM-B and JAM-C into Chinese hamster ovary cells, which are poorly permissive for reovirus infection. Both prototype and field-isolate reovirus strains were capable of infecting cells transfected with JAM-A but not those transfected with JAM-B or JAM-C. A sequence analysis of the {sigma}1-encoding S1 gene segment of the strains chosen for study revealed little conservation in the deduced {sigma}1 amino acid sequences among the three serotypes. This contrasts markedly with the observed sequence variability within each serotype, which is confined to a small number of amino acids. Mapping of these residues onto the crystal structure of {sigma}1 identified regions of conservation and variability, suggesting a likely mode of JAM-A binding via a conserved surface at the base of the {sigma}1 head domain.

* Corresponding author. Mailing address: Lamb Center for Pediatric Research, D7235 MCN, Vanderbilt University School of Medicine, Nashville, TN 37232. Phone: (615) 343-9943. Fax: (615) 343-9723. E-mail: terry.dermody{at}vanderbilt.edu.

Journal of Virology, July 2005, p. 7967-7978, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.7967-7978.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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