onr:"swepub:oai:lup.lub.lu.se:a62da20c-f3c2-4118-b8ea-ef3ef4635abd"
Search: onr:"swepub:oai:lup.lub.lu.se:a62da20c-f3c2-4118-b8ea-ef3ef4635abd" > Binding of vitronec...
- 1 of 1
- Previous record
- Next record
- To hitlist
- Kohler, S (author)
Binding of vitronectin and Factor H to Hic contributes to immune evasion of Streptococcus pneumoniae serotype 3.
- Article/chapterEnglish2015
Publisher, publication year, extent ...
- 2015
- electronicrdacarrier
Numbers
- LIBRIS-ID:oai:lup.lub.lu.se:a62da20c-f3c2-4118-b8ea-ef3ef4635abd
- https://lup.lub.lu.se/record/4699406URI
- https://doi.org/10.1160/TH14-06-0561DOI
Supplementary language notes
- Language:English
- Summary in:English
Part of subdatabase
- SwePubSwePub
Classification
Notes
- Streptococcus pneumoniae serotype 3 strains are highly resistant to opsonophagocytosis due to recruitment of the complement inhibitor Factor H via Hic, a member of the pneumococcal surface protein C (PspC) family. In this study, we demonstrated that Hic also interacts with vitronectin, a fluid-phase regulator involved in haemostasis, angiogenesis, and the terminal complement cascade as well as a component of the extracellular matrix. Blocking of Hic by specific antiserum or genetic deletion significantly reduced pneumococcal binding to soluble and immobilised vitronectin and to Factor H, respectively. In parallel, ectopic expression of Hic on the surface of Lactococcus lactis conferred binding to soluble and immobilised vitronectin as well as Factor H. Molecular analyses with truncated Hic fragments narrowed down the vitronectin-binding site to the central core of Hic (aa 151-201). This vitronectin-binding region is separate from that of Factor H, which binds to the N-terminus of Hic (aa 38-92). Binding of pneumococcal Hic was localised to the C-terminal heparin-binding domain (HBD3) of vitronectin. However, an N-terminal region to HBD3 was further involved in Hic-binding to immobilised vitronectin. Finally, vitronectin bound to Hic was functionally active and inhibited formation of the terminal complement complex. In conclusion, Hic interacts with vitronectin and simultaneously with Factor H, and both human proteins may contribute to colonisation and invasive disease caused by serotype 3 pneumococci.
Subject headings and genre
Added entries (persons, corporate bodies, meetings, titles ...)
- Hallström, T (author)
- Singh, BirendraLund University,Lunds universitet,Klinisk mikrobiologi, Malmö,Forskargrupper vid Lunds universitet,Clinical Microbiology, Malmö,Lund University Research Groups(Swepub:lu)med-bas (author)
- Riesbeck, KristianLund University,Lunds universitet,Klinisk mikrobiologi, Malmö,Forskargrupper vid Lunds universitet,Clinical Microbiology, Malmö,Lund University Research Groups(Swepub:lu)mikr-kri (author)
- Sparta, G (author)
- Zipfel, P F (author)
- Hammerschmidt, S (author)
- Klinisk mikrobiologi, MalmöForskargrupper vid Lunds universitet (creator_code:org_t)
Related titles
- In:Thrombosis and Haemostasis113:1, s. 125-1420340-6245
Internet link
Find in a library
- Thrombosis and Haemostasis (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Kohler, S
- Hallström, T
- Singh, Birendra
- Riesbeck, Kristi ...
- Sparta, G
- Zipfel, P F
- show more...
- Hammerschmidt, S
- show less...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Clinical Medicin ...
- and Cardiac and Card ...
- Articles in the publication
- Thrombosis and H ...
- By the university
- Lund University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
