Volltext-Downloads (blau) und Frontdoor-Views (grau)
The search result changed since you submitted your search request. Documents might be displayed in a different sort order.
  • search hit 28 of 30
Back to Result List

Bitte verwenden Sie diesen Link, wenn Sie dieses Dokument zitieren oder verlinken wollen: https://nbn-resolving.org/urn:nbn:de:gbv:9-opus-38250

Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria

  • A successful colonization of different compartments of the human host requires multifactorial contacts between bacterial surface proteins and host factors. Extracellular matrix proteins and matricellular proteins such as thrombospondin-1 play a pivotal role as adhesive substrates to ensure a strong interaction with pathobionts like the Gram-positive Streptococcus pneumoniae and Staphylococcus aureus. The human glycoprotein thrombospondin-1 is a component of the extracellular matrix and is highly abundant in the bloodstream during bacteremia. Human platelets secrete thrombospondin-1, which is then acquired by invading pathogens to facilitate colonization and immune evasion. Gram-positive bacteria express a broad spectrum of surface-exposed proteins, some of which also recognize thrombospondin-1. This review highlights the importance of thrombospondin-1 as an adhesion substrate to facilitate colonization, and we summarize the variety of thrombospondin-1-binding proteins of S. pneumoniae and S. aureus.

Download full text files

Export metadata

Additional Services

Search Google Scholar

Statistics

frontdoor_oas
Metadaten
Author: Ulrike Binsker, Thomas P. Kohler, Prof. Dr. Sven HammerschmidtORCiD
URN:urn:nbn:de:gbv:9-opus-38250
DOI:https://doi.org/10.1159/000496033
ISSN:1662-811X
ISSN:1662-8128
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/30814475
Parent Title (English):Journal of Innate Immunity
Publisher:S. Karger AG
Place of publication:Basel
Document Type:Article
Language:English
Date of first Publication:2019/02/27
Release Date:2022/04/04
Tag:Colonization; Dissemination; Human thrombospondin-1
GND Keyword:-
Volume:11
Issue:4
First Page:303
Last Page:315
Faculties:Mathematisch-Naturwissenschaftliche Fakultät / Interfakultäres Institut für Genetik und Funktionelle Genomforschung (MNF)
Licence (German):License LogoCreative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung