Literature DB >> 3048329

Host binding proteins and bacterial adhesion: ecology and binding model.

H Ceri1, Y Westra.   

Abstract

Defining the involvement of specific recognition and (or) adhesion molecules in the precise association formed between cells of an organism during development or between bacteria and specific host tissues has become a focus of extensive research. The possibility that the same molecules responsible for cellular adhesion in the host may also play a major role in determining host-bacterial interactions is now becoming more evident. The following review looks at the interaction of a group of host binding proteins, including lectins, fibronectin, and laminin, with respect to their specific association with bacteria. This information is dealt with both from the perspective of the ecology of the host and its autochthonous and pathogenic bacterial populations, as well as in terms of the difficulties in defining the nature of ligand associations even in the more simplified bacterial-host interaction.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3048329     DOI: 10.1139/o88-064

Source DB:  PubMed          Journal:  Biochem Cell Biol        ISSN: 0829-8211            Impact factor:   3.626


  1 in total

1.  Porphyromonas gingivalis fimbrillin is one of the fibronectin-binding proteins.

Authors:  Y Murakami; H Iwahashi; H Yasuda; T Umemoto; I Namikawa; S Kitano; S Hanazawa
Journal:  Infect Immun       Date:  1996-07       Impact factor: 3.441

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.