Vitronectin in bacterial pathogenesis: A host protein used in complement escape and cellular invasion.
Singh, Birendra LU ; Su, Shanice Yc LU and Riesbeck, Kristian LU
(2010)
In Molecular Microbiology
78(3).
p.545-560
- Abstract
- The multifunctional human glycoprotein vitronectin (Vn) plays a significant role in cell migration, tissue repair and regulation of membrane attack complex (MAC) formation. It also promotes neutrophil infiltration and, thus, enhances the inflammatory process during infection. In the host, a balanced homeostasis is maintained by Vn due to neutralization of the self-reactivity of the MAC. On the other hand, Vn bound to the bacterial surface protects from MAC mediated lysis and enhances adhesion. Gram-negative bacterial pathogens including Moraxella catarrhalis, Haemophilus influenzae, and Neisseria gonorrhoeae use Vn recruitment to prevent MAC deposition at their surface. Moreover, Gram-positive bacterial pathogens such as Streptococcus... (More)
- The multifunctional human glycoprotein vitronectin (Vn) plays a significant role in cell migration, tissue repair and regulation of membrane attack complex (MAC) formation. It also promotes neutrophil infiltration and, thus, enhances the inflammatory process during infection. In the host, a balanced homeostasis is maintained by Vn due to neutralization of the self-reactivity of the MAC. On the other hand, Vn bound to the bacterial surface protects from MAC mediated lysis and enhances adhesion. Gram-negative bacterial pathogens including Moraxella catarrhalis, Haemophilus influenzae, and Neisseria gonorrhoeae use Vn recruitment to prevent MAC deposition at their surface. Moreover, Gram-positive bacterial pathogens such as Streptococcus pneumoniae and S. pyogenes utilize Vn for effective adhesion to host cells and subsequent internalization. Vitronectin has an Arg-Gly-Asp (RGD) sequence for binding the host cell integrin receptors and a separate bacterial binding domain for pathogens, and thus more likely functions to cross-link bacteria and epithelial cells. Once bacteria are attached to the vitronectin-integrin complex, various host cell-signalling events are activated and promote internalization. In this review, we focus on the important roles of vitronectin in bacterial pathogenesis and describe different strategies used by pathogens to evade the host response by the help of this intriguing molecule. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1688681
- author
- Singh, Birendra
LU
; Su, Shanice Yc
LU
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Microbiology
- volume
- 78
- issue
- 3
- pages
- 545 - 560
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000283377600004
- pmid:20807208
- scopus:77958565410
- ISSN
- 1365-2958
- DOI
- 10.1111/j.1365-2958.2010.07373.x
- language
- English
- LU publication?
- yes
- id
- 48425ab4-9890-4d11-bab9-772252d6bbd5 (old id 1688681)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/20807208?dopt=Abstract
- date added to LUP
- 2016-04-04 07:43:59
- date last changed
- 2022-04-23 08:34:33
@article{48425ab4-9890-4d11-bab9-772252d6bbd5,
abstract = {{The multifunctional human glycoprotein vitronectin (Vn) plays a significant role in cell migration, tissue repair and regulation of membrane attack complex (MAC) formation. It also promotes neutrophil infiltration and, thus, enhances the inflammatory process during infection. In the host, a balanced homeostasis is maintained by Vn due to neutralization of the self-reactivity of the MAC. On the other hand, Vn bound to the bacterial surface protects from MAC mediated lysis and enhances adhesion. Gram-negative bacterial pathogens including Moraxella catarrhalis, Haemophilus influenzae, and Neisseria gonorrhoeae use Vn recruitment to prevent MAC deposition at their surface. Moreover, Gram-positive bacterial pathogens such as Streptococcus pneumoniae and S. pyogenes utilize Vn for effective adhesion to host cells and subsequent internalization. Vitronectin has an Arg-Gly-Asp (RGD) sequence for binding the host cell integrin receptors and a separate bacterial binding domain for pathogens, and thus more likely functions to cross-link bacteria and epithelial cells. Once bacteria are attached to the vitronectin-integrin complex, various host cell-signalling events are activated and promote internalization. In this review, we focus on the important roles of vitronectin in bacterial pathogenesis and describe different strategies used by pathogens to evade the host response by the help of this intriguing molecule.}},
author = {{Singh, Birendra and Su, Shanice Yc and Riesbeck, Kristian}},
issn = {{1365-2958}},
language = {{eng}},
number = {{3}},
pages = {{545--560}},
publisher = {{Wiley-Blackwell}},
series = {{Molecular Microbiology}},
title = {{Vitronectin in bacterial pathogenesis: A host protein used in complement escape and cellular invasion.}},
url = {{http://dx.doi.org/10.1111/j.1365-2958.2010.07373.x}},
doi = {{10.1111/j.1365-2958.2010.07373.x}},
volume = {{78}},
year = {{2010}},
}