Literature DB >> 22222876

Bacterial hydrolysis of host glycoproteins - powerful protein modification and efficient nutrient acquisition.

Julia Garbe1, Mattias Collin.   

Abstract

Glycoproteins are ubiquitous in nature and fundamental to most biological processes, including the human immune system. The glycoprotein carbohydrate moieties, or glycans, are very diverse in their structure and composition, and have major effects on the chemical, physical and biological properties of these glycoproteins. The hydrolysis of glycoprotein glycans by bacterial glycosidases can have dramatic effects on glycoprotein function and, thereby, be beneficial for the bacteria in different ways. This review gives an introduction to the expanding field of extracellular glycosidases from bacterial pathogens with activity on host glycoproteins, describes some known and proposed consequences for the host and the bacteria and discusses some evolutionary and regulatory aspects of bacterial glycosidases.
Copyright © 2012 S. Karger AG, Basel.

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Year:  2012        PMID: 22222876      PMCID: PMC6741532          DOI: 10.1159/000334775

Source DB:  PubMed          Journal:  J Innate Immun        ISSN: 1662-811X            Impact factor:   7.349


  17 in total

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6.  EndoS and EndoS2 hydrolyze Fc-glycans on therapeutic antibodies with different glycoform selectivity and can be used for rapid quantification of high-mannose glycans.

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7.  EndoE from Enterococcus faecalis hydrolyzes the glycans of the biofilm inhibiting protein lactoferrin and mediates growth.

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