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Volume 154, Issue 8

The binding of to immobilized laminin-1 and its role in the cytotoxicity exerted by the parasite Free

Abstract

The recognition and binding of pathogens to extracellular matrix glycoproteins may determine the outcome of infective processes. The interaction between the bovine urogenital parasite and the major basal membrane glycoprotein laminin-1 (LMN-1) was investigated. The chemical nature of parasite molecules involved in the attachment of to immobilized LMN-1 and the influence of LMN-1 in the toxicity exerted by the parasite to HeLa cells was studied. Attachment of to LMN-1 resulted in notable morphological alterations of the parasite, which became amoeboid. recognized LMN-1 through specific amino acid sequences (AG73, C16, A208 and A13) in the LMN-1 molecule, and the protein nature of the parasite molecules involved in the recognition was demonstrated by dot-blot analyses. Such molecular recognition was cation-dependent and five LMN-1-binding molecules (220, 200, 130, 125 and 80 kDa) were identified in . Binding of to LMN-1 rendered the parasite toxic to HeLa cell monolayers. Thus, LMN-1 appears to provide signalling cues that mediate important cell functions in concerning its interaction with host cells.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): ECM, extracellular matrix and LMN-1. laminin-1
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2008-08-01
2024-05-03
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The binding of Tritrichomonas foetus to immobilized laminin-1 and its role in the cytotoxicity exerted by the parasite
Microbiology 154, 2283 (2008); https://doi.org/10.1099/mic.0.2007/015941-0
/content/journal/micro/10.1099/mic.0.2007/015941-0
/content/journal/micro/10.1099/mic.0.2007/015941-0
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