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Vitronectin in bacterial pathogenesis: A host protein used in complement escape and cellular invasion.

Singh, Birendra LU ; Su, Yu-Ching and Riesbeck, Kristian LU (2010) In Molecular Microbiology Oct. 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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
Oct
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
2010-10-03 19:21:11
date last changed
2018-06-03 04:30:37
@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, Yu-Ching and Riesbeck, Kristian},
  issn         = {1365-2958},
  language     = {eng},
  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},
  volume       = {Oct},
  year         = {2010},
}