Results 141 to 150 of about 1,564,390 (179)

Secretion of type-1-fimbriae binding proteins from human neutrophil granulocytes

open access: yesInflammation, 1996
Granule matrix proteins secreted from human neutrophils after ionomycin stimulation were separated by SDS-PAGE, blotted onto a polyvinylidene diflouride (PVDF) membrane and overlaid with the mannose-binding lectin concanavalin A (Con A) or Escherichia coli bacteria exposing type-I-fimbriae.
A, Karlsson, C, Dahlgren
openaire   +3 more sources

Structural and antigenic characterization of a novel genotype of Mfa1 fimbriae in Porphyromonas gingivalis

open access: yesJournal of Oral Microbiology, 2023
Background Mfa1 fimbriae of the periodontal pathogen Porphyromonas gingivalis are responsible for biofilm formation and comprise five proteins: Mfa1–5. Two major genotypes, mfa170 and mfa153, encode major fimbrillin.
Yoshiaki Hasegawa   +2 more
exaly   +2 more sources

Binding of Enterobacterial Fimbria to Proteins of Basement Membranes and Connective Tissue — A Novel Function for Fimbriae

1991
Fimbriae are important virulence factors in a number of enterobacterial infections. It is generally thought that they increase the pathogenic potential of bacteria by mediating adherence to glycoconjugates of host epithelia, thus giving resistance to mechanical clearance defense systems of the body.
Timo K. Korhonen   +10 more
openaire   +1 more source

Fimbriae of Bacteroides nodosus: protein engineering of the structural subunit for the production of an exogenous peptide

"Protein Engineering, Design and Selection", 1989
The pattern of sequence variation between Bacteroides nodosus fimbrial subunits of different serotypes suggests a degree of flexibility, which might be exploited for protein engineering approaches for the expression of other peptides. We have tested this using the well-characterized peptide epitope from VP1 of foot-and-mouth disease virus (FMDV ...
Jennings, P. A.   +3 more
openaire   +4 more sources

Cloning and sequence analysis of the fimbriae associated protein (fap) gene fromActinobacillus actinomycetemcomitans

Microbial Pathogenesis, 1997
Fimbrial-associated protein, an attachment factor of Actinobacillus actinomycetemcomitans, was genetically analysed by cloning. The plasmid obtained was found to harbor a 1.7kb fragment which contained a 228bp open reading frame encoding 76 amino acids (7.970kDa).
K, Ishihara   +4 more
openaire   +2 more sources

Formulation and characterisation of Bordetella pertussis fimbriae as novel carrier proteins for Hib conjugate vaccines

Vaccine, 2001
Haemophilus influenzae type b (Hib) capsular polysaccharide (polyribosylribitol phosphate, PRP) is the active component of conjugate vaccines that have proven successful in preventing invasive Hib disease. Conjugation of PRP to a protein carrier greatly improves its immunogenicity providing protection in infants and subsequent antibody maturation upon ...
A, Crowley-Luke   +4 more
openaire   +2 more sources

Extracellular protein fibrils in Chrysochromulina breviturrita (Prymnesiophyceae) and their serological relationship to fungal fimbriae

Archives of Microbiology, 1986
An extensive network of extracellular fibrils was revealed by negative staining in the greenish gold algal flagellate, Chrysochromulina breviturrita. These fibrils were of uniform diameter (4–5 nm), sometimes exceeding 5 μm in length. In addition there were short, narrower fibrils (2–3 nm) on the surface of the flagella. Six protein bands were isolated
A. W. Day, R. B. Gardiner, L. M. Brown
openaire   +1 more source

Localization and function of the accessory protein Mfa3 in Porphyromonas gingivalis Mfa1 fimbriae

Molecular Oral Microbiology, 2013
SummaryThe fimbriae of Porphyromonas gingivalis, the causative agent of periodontitis, have been implicated in various aspects of pathogenicity, such as colonization, adhesion and aggregation. Porphyromonas gingivalis ATCC 33277 has two adhesins comprised of the FimA and Mfa1 fimbriae.
Y, Hasegawa   +8 more
openaire   +2 more sources

Mechanism of pathogen‐specific TLR4 activation in the mucosa: Fimbriae, recognition receptors and adaptor protein selection

European Journal of Immunology, 2006
AbstractThe mucosal host defence discriminates pathogens from commensals, and prevents infection while allowing the normal flora to persist. Paradoxically, Toll‐like receptors (TLR) control the mucosal defence against pathogens, even though the TLR recognise conserved molecules like LPS, which are shared between pathogens and commensals.
Hans, Fischer   +4 more
openaire   +2 more sources

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