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Journal of Virology, November 2002, p. 10972-10979, Vol. 76, No. 21
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.21.10972-10979.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Multiple Functions of Immunoglobulin A in Mucosal Defense against Viruses: an In Vitro Measles Virus Model

Huimin Yan,1 Michael E. Lamm,1 Ewa Björling,2,3 and Yung T. Huang1,4*

Institute of Pathology, Case Western Reserve University,1 Department of Pathology, University Hospitals of Cleveland, Cleveland, Ohio 44106,4 Microbiology and Tumor Biology Center, Karolinska Institutet, S-171 77 Stockholm,2 Research Center, The South Hospital, Karolinska Institutet, S-118 83 Stockholm, Sweden3

Received 22 April 2002/ Accepted 23 July 2002

Three defense functions of immunoglobulin A (IgA), immune exclusion, intracellular neutralization, and virus excretion, were assessed in a measles virus model using polarized epithelial cells expressing the polymeric immunoglobulin receptor and monoclonal antibodies against the viral H and F envelope proteins and the internal N protein. Anti-H IgA was the most effective antibody at preventing infection via the apical surface, i.e., immune exclusion. This IgA was also the most effective at intraepithelial cell neutralization after infection at the apical surface and endocytosis of IgA at the basolateral surface, although an antibody against the internal N protein was also effective. In the intracellular neutralization experiments, confocal immunofluorescence microscopy showed prominent colocalization of anti-H IgA and H protein inside virus-infected cells, whereas colocalization of anti-F and F protein and of anti-N and N protein was much less, in agreement with the neutralization results. Combinations of IgA anti-H, anti-F, and anti-N showed no synergistic effects in intracellular neutralization. In the immune excretion experiments, virus immune complexes with either anti-H or anti-F IgA placed beneath polarized epithelial cells could be transported to the apical supernatant. Anti-F IgA, which was relatively poor at immune exclusion and intracellular neutralization, was the most robust at virus excretion. Thus, the studies collectively demonstrated three different antiviral functions of IgA in relation to epithelium and also suggested that the particular viral component with which a given IgA antibody reacts is an important determinant of the magnitude of the antiviral effect.

* Corresponding author. Mailing address: Institute of Pathology, Case Western Reserve University, Cleveland, OH 44106. Phone: (216) 844-8611. Fax: (216) 368-0495. E-mail: yth{at}po.cwru.edu.

Journal of Virology, November 2002, p. 10972-10979, Vol. 76, No. 21
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.21.10972-10979.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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