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Comparative innate immune interactions of human and bovine secretory IgA with pathogenic and non-pathogenic bacteria
Affiliation:1. Department of Obstetrics and Gynecology, Hanyang University Guri Hospital, College of Medicine, Gyeonggi Province 471-701, Republic of Korea;2. Department of Environmental Biology and Medical Parasitology, Hanyang University College of Medicine, Seoul 133-791, Republic of Korea;3. Department of Environmental Medical Biology, Institute of Tropical Medicine, Yonsei University College of Medicine, Seoul 120-752, Republic of Korea;4. Department of Biochemistry & Molecular Biology, Hanyang University College of Medicine, Seoul 133-791, Republic of Korea;5. Department of Preventive Medicine, College of Medicine, Dong-A University, Busan 602-715, Republic of Korea;6. Department of Parasitology, School of Medicine, Kyungpook National University, Daegu 700-422, Republic of Korea
Abstract:Secretory IgA (SIgA) from milk contributes to early colonization and maintenance of commensal/symbiotic bacteria in the gut, as well as providing defence against pathogens. SIgA binds bacteria using specific antigenic sites or non-specifically via its glycans attached to α-heavy-chain and secretory component. In our study, we tested the hypothesis that human and bovine SIgA have similar innate-binding activity for bacteria. SIgAs, isolated from human and bovine milk, were incubated with a selection of commensal, pathogenic and probiotic bacteria. Using flow cytometry, we measured numbers of bacteria binding SIgA and their level of SIgA binding. The percentage of bacteria bound by human and bovine SIgA varied from 30 to 90% depending on bacterial species and strains, but was remarkably consistent between human and bovine SIgA. The level of SIgA binding per bacterial cell was lower for those bacteria that had a higher percentage of SIgA-bound bacteria, and higher for those bacteria that had lower percentage of SIgA-bound bacteria. Overall, human and bovine SIgA interacted with bacteria in a comparable way. This contributes to longer term research about the potential benefits of bovine SIgA for human consumers.
Keywords:Secretory IgA  Bovine IgA  Human IgA  Bacteria  Bacteria binding
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