Bacterial Hydrolysis of Host Glycoproteins - Powerful Protein Modification and Efficient Nutrient Acquisition.
Garbe, Julia LU and Collin, Mattias LU
(2012)
In Journal of Innate Immunity
4(2).
p.121-131
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2336645
- author
- Garbe, Julia
LU
and Collin, Mattias
LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Innate Immunity
- volume
- 4
- issue
- 2
- pages
- 121 - 131
- publisher
- Karger
- external identifiers
-
- wos:000300758400002
- pmid:22222876
- scopus:84857792795
- pmid:22222876
- ISSN
- 1662-811X
- DOI
- 10.1159/000334775
- language
- English
- LU publication?
- yes
- id
- 445455a9-78eb-423a-9234-0dc9917bccf1 (old id 2336645)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/22222876?dopt=Abstract
- date added to LUP
- 2016-04-01 09:54:49
- date last changed
- 2022-02-17 04:49:06
@article{445455a9-78eb-423a-9234-0dc9917bccf1,
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.}},
author = {{Garbe, Julia and Collin, Mattias}},
issn = {{1662-811X}},
language = {{eng}},
number = {{2}},
pages = {{121--131}},
publisher = {{Karger}},
series = {{Journal of Innate Immunity}},
title = {{Bacterial Hydrolysis of Host Glycoproteins - Powerful Protein Modification and Efficient Nutrient Acquisition.}},
url = {{https://lup.lub.lu.se/search/files/1383476/2373856.pdf}},
doi = {{10.1159/000334775}},
volume = {{4}},
year = {{2012}},
}