Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Host cell invasion by Plasmodium falciparum requires multiple molecular interactions between host receptors and parasite ligands. A family of parasite proteins, which contain the conserved thrombospondin structural repeat motif (TSR), has been implicated in receptor binding during invasion. In this study we have characterized the functional role of a TSR containing blood stage protein referred to as P. falciparum thrombospondin related apical merozoite protein (PfTRAMP). Both native and recombinant PfTRAMP bind untreated as well as neuraminidase, trypsin or chymotrypsin-treated human erythrocytes. PfTRAMP is localized in the rhoptry bulb and is secreted during invasion. Adhesion of microneme protein EBA175 with its erythrocyte receptor glycophorin A provides the signal that triggers release of PfTRAMP from the rhoptries. Rabbit antibodies raised against PfTRAMP block erythrocyte invasion by P. falciparum suggesting that PfTRAMP plays an important functional role in invasion. Combination of antibodies against PfTRAMP with antibodies against microneme protein EBA175 provides an additive inhibitory effect against invasion. These observations suggest that targeting multiple conserved parasite ligands involved in different steps of invasion may provide an effective strategy for the development of vaccines against blood stage malaria parasites.
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PMID:A thrombospondin structural repeat containing rhoptry protein from Plasmodium falciparum mediates erythrocyte invasion. 2338 21

Adhesion of oral mitis group streptococci, such as Streptococcus gordonii, to acquired pellicle on the tooth surface is the first step in oral biofilm formation. S. gordonii strain DL1 possesses an Hsa adhesin, which recognizes the terminal sialic acid of host sialoglycoconjugates. The aim of the present study was to investigate the role of the Hsa adhesin in biofilm formation. The biofilm-forming ability of a S. gordonii hsa mutant on microtiter plates pre-coated with saliva, fetuin, or mucin was significantly lower than that of wild-type strain DL1. In contrast, no significant difference in biofilm-forming ability was observed in plates pre-coated with bovine serum albumin, which does not contain sialic acid. The biofilm-forming ability of strain DL1 in saliva-coated microtiter plates was also significantly reduced when the plate was pre-treated with neuraminidase. The sialic acid-dependent biofilm-forming ability of different wild-type S. gordonii strains varied. However, Southern and western blot analyses showed that all the tested wild-type strains possessed and expressed hsa homologs, respectively. These results indicate that the binding of Hsa adhesin to sialoglycoconjugates is associated with biofilm formation of S. gordonii DL1, and imply variation in the contribution of Hsa and its homologs to S. gordonii biofilm formation.
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PMID:Contribution of Streptococcus gordonii Hsa Adhesin to Biofilm Formation. 2800 5


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