The Nontypeable Haemophilus influenzae Major Adhesin Hia Is a Dual-Function Lectin That Binds to Human-Specific Respiratory Tract Sialic Acid Glycan Receptors

Author:

Atack John M.1ORCID,Day Christopher J.1,Poole Jessica1,Brockman Kenneth L.2,Timms Jamie R. L.1,Winter Linda E.3,Haselhorst Thomas1,Bakaletz Lauren O.2ORCID,Barenkamp Stephen J.3,Jennings Michael P.1ORCID

Affiliation:

1. Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia

2. Center for Microbial Pathogenesis, The Research Institute at Nationwide Children’s Hospital and The Ohio State University College of Medicine, Columbus, Ohio, USA

3. Department of Pediatrics, Saint Louis University School of Medicine, and the Pediatric Research Institute, Cardinal Glennon Children’s Medical Center, Saint Louis, Missouri, USA

Abstract

Host-adapted bacterial pathogens like NTHi have evolved specific mechanisms to colonize their restricted host niche. Relatively few of the adhesins expressed by NTHi have been characterized as regards their binding affinity at the molecular level. In this work, we show that the major NTHi adhesin Hia preferentially binds to Neu5Ac-α2-6-sialyllactosamine, the form of sialic acid expressed in humans. The receptors targeted by Hia in the human airway mirror those targeted by influenza A virus and indicates the broad importance of sialic acid glycans as receptors for microbes that colonize the human airway.

Funder

HHS | National Institutes of Health

Department of Health, Australian Government | National Health and Medical Research Council

Australian Research Council

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

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