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Journal of Virology, August 2004, p. 8565-8572, Vol. 78, No. 16
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.16.8565-8572.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Pulmonary Collectins Modulate Strain-Specific Influenza A Virus Infection and Host Responses

Samuel Hawgood,1* Cynthia Brown,1 Jess Edmondson,1 Amber Stumbaugh,1 Lennell Allen,1 Jon Goerke,1 Howard Clark,2 and Francis Poulain1,{dagger}

Department of Pediatrics and Cardiovascular Research Institute, University of California-San Francisco, San Francisco, California 94118-1245,1 M.R.C. Immunochemistry Unit, University of Oxford, Oxford, United Kingdom OX1 3QU2

Received 14 December 2003/ Accepted 30 March 2004

Collectins are secreted collagen-like lectins that bind, agglutinate, and neutralize influenza A virus (IAV) in vitro. Surfactant proteins A and D (SP-A and SP-D) are collectins expressed in the airway and alveolar epithelium and could have a role in the regulation of IAV infection in vivo. Previous studies have shown that binding of SP-D to IAV is dependent on the glycosylation of specific sites on the HA1 domain of hemagglutinin on the surface of IAV, while the binding of SP-A to the HA1 domain is dependent on the glycosylation of the carbohydrate recognition domain of SP-A. Here, using SP-A and SP-D gene-targeted mice on a common C57BL6 background, we report that viral replication and the host response as measured by weight loss, neutrophil influx into the lung, and local cytokine release are regulated by SP-D but not SP-A when the IAV is glycosylated at a specific site (N165) on the HA1 domain. SP-D does not protect against IAV infection with a strain lacking glycosylation at N165. With the exception of a small difference on day 2 after infection with X-79, we did not find any significant difference in viral load in SP-A–/– mice with either IAV strain, although small differences in the cytokine responses to IAV were detected in SP-A–/– mice. Mice deficient in both SP-A and SP-D responded to IAV similarly to mice deficient in SP-D alone. Since most strains of IAV currently circulating are glycosylated at N165, SP-D may play a role in protection from IAV infection.

* Corresponding author. Mailing address: University of California-San Francisco, Laurel Heights Campus, 3333 California St., Suite 150, San Francisco, CA 94118-1944. Phone: (415) 476-2908. Fax: (415) 476-3586. E-mail: Hawgood{at}itsa.ucsf.edu.

{dagger} Present address: Division of Neonatology, University of California at Davis, Davis, CA 95616.

Journal of Virology, August 2004, p. 8565-8572, Vol. 78, No. 16
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.16.8565-8572.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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