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1 Department of Medicine, Section Hematology/Oncology, Boston University School of Medicine, Boston, MA, USA
2 Department of Biochemistry and Cell Biology and Graduate School of Animal Health, Utrecht University, Utrecht, The Netherlands
3 Department of Pathology, Washington University School of Medicine, St. Louis, MO, USA
4 Medical Technology Center, University of Southern Denmark, Odense, Denmark
* To whom correspondence should be addressed. E-mail: khartsho{at}bu.edu.
The surfactant collectins, surfactant proteins A and D (SP-A and D) and scavenger receptor rich glycoprotein gp-340 (gp-340) inhibit influenza A virus (IAV) in the following order of potency: SP-D>gp-340>SP-A. SP-D binds in a calcium-dependent manner to carbohydrate attachments on the viral hemagglutinin (HA) and neuraminidase (NA). By contrast, gp-340 and SP-A act like mucins in that they provide sialic acid ligands which bind to the viral HA. In this study, SP-D, SP-A and gp-340 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 gp-340 and SP-D was further characterized using monoclonal antibodies. Although gp-340 can bind to SP-D at a site distinct from the mannan-binding site, binding of gp-340 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 (BAL) fluid. Hence, oseltamivir collaborates with innate immune proteins in inhibiting the initial infection of epithelial cells.
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