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 |