Disease relevance of fimX

• Nucleotide sequence of the fim3 gene from Bordetella pertussis and homology to fim2 and fimX gene products [1].
• Fimbrial phase variation in Bordetella pertussis: a novel mechanism for transcriptional regulation [2].
• These constructs did not result in the expression of fimbrial subunit at detectable levels in several E. coli strains including DH5 [3].
• A fimbrial mutant was analysed in a mouse respiratory infection model, together with a strain harbouring a deletion in the gene for the filamentous haemagglutinin [4].
• Homology was observed between the N-termini of these polypeptides, and fimbrial subunits from Escherichia coli, Haemophilus influenzae and Proteus mirabilis [5].

High impact information on fimX

• Its amino acid sequence shares similarities with those of the fimbrial subunits [6].
• We propose that these mutations affect transcription of the fim genes by varying the distance between the binding site for an activator and the -10 box [2].
• Nonopsonized Bordetella pertussis bind to human monocytes by means of the virulence factors filamentous hemagglutinin (FHA), pertactin, and the minor fimbrial subunit FimD [7].
• The primary structure of FimD, derived from the DNA sequence of its gene, showed homology with a number of fimbrial adhesins [8].
• An insertion mutation in fimB abolished the expression of fimbrial subunits, implicating this gene in the biosynthesis of both serotype 2 and 3 fimbriae [9].

Chemical compound and disease context of fimX

• Mouse-protecting and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis [10].

Biological context of fimX

• In this communication we present the cloning and nucleotide sequence of the fimX gene and its homology to the fim2 gene [11].
• Analysis of PhoA activity indicated that the fimbrial gene cluster was positively regulated by the bvg locus [9].
• A search for pilin genes in a Bordetella pertussis (Bp) genomic library has led to the identification of several clones which hybridize to synthetic oligonucleotides with sequences derived from amino acid sequences of Bp fimbrial subunits [11].
• The construction of a phylogenetic tree suggested that fimA may be the primordial major fimbrial subunit gene from which the other three were derived by gene duplication [9].
• As such, FimN may be a previously overlooked fimbrial antigen and may play an important role in the pathogenicity of B. bronchiseptica [12].

Anatomical context of fimX

• The ability of the two fimbrial mutants to colonize the nasopharynx, trachea, and lungs was compared with those of the wild type parental strain and a filamentous hemagglutinin (FHA) mutant [13].
• These subunits are connected by interactions along the fimbrial backbone which, unlike other classes of bacterial fimbriae, has no axial channel [14].
• The results obtained with the two types of fimbrial subunits were generally the same: a recombinant protein of the expected molecular mass (19.2 kDa) was present in the periplasm of the leaky mutants and of CAG629 strain (Ion protease- and heat shock protease-deficient) [15].

Associations of fimX with chemical compounds

• The protein deduced from the nucleotide sequence shows good agreement with the NH2-terminal amino acid sequence, amino acid composition and molecular weight of the purified fimbrial subunit [16].
• The fimbrial agglutinogens recognized by the monoclonal antibodies were also uniquely reactive with either U.S. Reference Factor 2 or 6 antiserum (Eldering agglutinogen 2 or 6 polyclonal antiserum) in an indirect ELISA [17].
• The major heparin binding regions identified in Fim2 are part of epitopes recognized by human antibodies, suggesting that the heparin binding regions are exposed at the fimbrial surface and are immunodominant [18].
• By Western blot (immunoblot), it was determined that monoclonal antibody CF8 does not react with proteins denatured by treatment with sodium dodecyl sulfate and beta-mercaptoethanol and by boiling for 5 min but that it does recognize fimbrial proteins in their native, nondenatured state [19].
• These include genes coding for the synthesis of a polysaccharide capsule, hemagglutinins, a type I secretion system adjacent to two very large genes for secreted proteins, and unique genes for both lipopolysaccharide and fimbrial biogenesis [20].

Other interactions of fimX

• It also has an activator binding region, upstream from the C-stretch, that closely resembles a corresponding bvg regulated region in fim2, fim3, and fimX [12].
• We determined the frequency of variants of B. pertussis pertactin (prn), and pertussis toxin subunit 1 (ptxS1) genes, restriction fragment length polymorphism (RFLP) types and fimbrial serotypes prevalent in Australia prior to, and during the 1990s [21].

Analytical, diagnostic and therapeutic context of fimX

• However, such antibodies reacted in Western blots equally well with the recombinant and wild-type form of the fimbrial subunit.(ABSTRACT TRUNCATED AT 250 WORDS)[3]
• GMCs of maternal antibodies at delivery (ELISA units/mL) were 2.4 for PT, 6.9 for FHA, and 13 for FIM [22].
• We used Southern blot analysis with a 30-mer specific for the fimbrial sequences [23].
• Using immunoelectron microscopy, we provide evidence that FimD is located at the fimbrial tip [13].
• Purification and crystallization of fimbrial hemagglutinin from Bordetella pertussis [24].

References