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Fish pathogen binding to mucins from Atlantic salmon and Arctic char differs in avidity and specificity and is modulated by fluid velocity

Journal article
Authors János T Padra
Abarna V M Murugan
Kristina Sundell
Henrik Sundh
John Benktander
Sara K. Lindén
Published in PLoS ONE
Volume 14
Issue 5
Pages e0215583
ISSN 1932-6203
Publication year 2019
Published at Department of Biological and Environmental Sciences
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages e0215583
Language en
Links dx.doi.org/10.1371/journal.pone.021...
Keywords aeromonas-hydrophila, vibrio-harveyi, rainbow-trout, helicobacter-pylori, yersinia-ruckeri, winter ulcer, salar l, infection, skin, identification, Science & Technology - Other Topics, ttal kr, 1980, canadian journal of microbiology, v26, p1501
Subject categories Microbiology

Abstract

Disease outbreaks are limiting factors for an ethical and economically sustainable aquaculture industry. The first point of contact between a pathogen and a host occurs in the mucus, which covers the epithelial surfaces of the skin, gills and gastrointestinal tract. Increased knowledge on host-pathogen interactions at these primary barriers may contribute to development of disease prevention strategies. The mucus layer is built of highly glycosylated mucins, and mucin glycosylation differs between these epithelial sites. We have previously shown that A. salmonicida binds to Atlantic salmon mucins. Here we demonstrate binding of four additional bacteria, A. hydrophila, V. harveyi, M. viscosa and Y. ruckeri, to mucins from Atlantic salmon and Arctic char. No specific binding could be observed for V. salmonicida to any of the mucin groups. Mucin binding avidity was highest for A. hydrophila and A. salmonicida, followed by V. harveyi, M. viscosa and Y. ruckeri in decreasing order. Four of the pathogens showed highest binding to either gills or intestinal mucins, whereas none of the pathogens had preference for binding to skin mucins. Fluid velocity enhanced binding of intestinal mucins to A. hydrophila and A. salmonicida at 1.5 and 2 cm/s, whereas a velocity of 2 cm/s for skin mucins increased binding of A. salmonicida and decreased binding of A. hydrophila. Binding avidity, specificity and the effect of fluid velocity on binding thus differ between salmonid pathogens and with mucin origin. The results are in line with a model where the short skin mucin glycans contribute to contact with pathogens whereas pathogen binding to mucins with complex glycans aid the removal of pathogens from internal epithelial surfaces.

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