The Sialic Acid Binding Activity of Human Parainfluenza Virus 3 and Mumps Virus Glycoproteins Enhances the Adherence of Group B Streptococci to HEp-2 Cells

Bibliographic Details
Title: The Sialic Acid Binding Activity of Human Parainfluenza Virus 3 and Mumps Virus Glycoproteins Enhances the Adherence of Group B Streptococci to HEp-2 Cells
Authors: Jie Tong, Yuguang Fu, Fandan Meng, Nadine Krüger, Peter Valentin-Weigand, Georg Herrler
Source: Frontiers in Cellular and Infection Microbiology, Vol 8 (2018)
Publisher Information: Frontiers Media S.A., 2018.
Publication Year: 2018
Collection: LCC:Microbiology
Subject Terms: sialic acids, hemagglutinin-neuraminidase protein, parainfluenza virus, mumps virus, group B streptococci, co-infection, Microbiology, QR1-502
More Details: In the complex microenvironment of the human respiratory tract, different kinds of microorganisms may synergistically interact with each other resulting in viral-bacterial co-infections that are often associated with more severe diseases than the respective mono-infections. Human respiratory paramyxoviruses, for example parainfluenza virus type 3 (HPIV3), are common causes of respiratory diseases both in infants and a subset of adults. HPIV3 recognizes sialic acid (SA)-containing receptors on host cells. In contrast to human influenza viruses which have a preference for α2,6-linked sialic acid, HPIV3 preferentially recognize α2,3-linked sialic acids. Group B streptococci (GBS) are colonizers in the human respiratory tract. They contain a capsular polysaccharide with terminal sialic acid residues in an α2,3-linkage. In the present study, we report that HPIV3 can recognize the α2,3-linked sialic acids present on GBS. The interaction was evident not only by the binding of virions to GBS in a co-sedimentation assay, but also in the GBS binding to HPIV3-infected cells. While co-infection by GBS and HPIV3 had a delaying effect on the virus replication, it enhanced GBS adherence to virus-infected cells. To show that other human paramyxoviruses are also able to recognize the capsular sialic acid of GBS we demonstrate that GBS attaches in a sialic acid-dependent way to transfected BHK cells expressing the HN protein of mumps virus (MuV) on their surface. Overall, our results reveal a new type of synergism in the co-infection by respiratory pathogens, which is based on the recognition of α2,3-linked sialic acids. This interaction between human paramyxoviruses and GBS enhances the bacterial adherence to airway cells and thus may result in more severe disease.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2235-2988
Relation: https://www.frontiersin.org/article/10.3389/fcimb.2018.00280/full; https://doaj.org/toc/2235-2988
DOI: 10.3389/fcimb.2018.00280
Access URL: https://doaj.org/article/d6e374bf950c454281da056fad5a881e
Accession Number: edsdoj.6e374bf950c454281da056fad5a881e
Database: Directory of Open Access Journals
More Details
ISSN:22352988
DOI:10.3389/fcimb.2018.00280
Published in:Frontiers in Cellular and Infection Microbiology
Language:English