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This Article Full Text Full Text (PDF) All Versions of this Article: 288/5/L831    most recent 00365.2004v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (9) Citing Articles via Google Scholar Google Scholar Articles by White, M. R. Articles by Hartshorn, K. L. Search for Related Content PubMed PubMed Citation Articles by White, M. R. Articles by Hartshorn, K. L.

Cooperative anti-influenza activities of respiratory innate immune proteins and neuraminidase inhibitor

¹Department of Medicine, Section of Hematology/Oncology, Boston University School of Medicine, Boston, Massachusetts ²Department of Pathology, Washington University School of Medicine, St. Louis, Missouri ³Department of Biochemistry and Cell Biology and Graduate School of Animal Health, Utrecht University, Utrecht, The Netherlands ⁴Medical Biotechnology Center, University of Southern Denmark, Odense, Denmark

Submitted 27 September 2004 ; accepted in final form 29 November 2004

The surfactant collectins, surfactant proteins A and D (SP-A and D), and scavenger receptor-rich glycoprotein 340 (gp340) inhibit influenza A virus (IAV) in the following order of potency: SP-D>gp340>SP-A. SP-D binds in a calcium-dependent manner to carbohydrate attachments on the viral hemagglutinin (HA) and neuraminidase (NA). By contrast, gp340 and SP-A act like mucins in that they provide sialic acid ligands that bind to the viral HA. In this study, SP-D, SP-A, and gp340 showed cooperative antiviral interactions. These cooperative effects were most evident in viral aggregation but were also observed in at least some hemagglutination inhibition and viral neutralization assays. The mechanism of binding between gp340 and SP-D was further characterized using monoclonal antibodies. Although gp340 can bind to SP-D at a site distinct from the mannan-binding site, binding of gp340 to SP-D did not contribute to cooperative antiviral interactions. SP-D and mucin showed cooperative interactions, apparently dependent on NA inhibition by SP-D. The commercial NA inhibitor oseltamivir had a similar effect and also enhanced the neutralizing activity of SP-A and bronchoalveolar lavage fluid. Hence, oseltamivir collaborates with innate immune proteins in inhibiting the initial infection of epithelial cells.

surfactant protein D; surfactant protein A; gp340; oseltamivir

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