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Journal articles on the topic 'Proteinas fimbriais'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Zeiner, Sarah A., Brett E. Dwyer, and Steven Clegg. "FimA, FimF, and FimH Are Necessary for Assembly of Type 1 Fimbriae on Salmonella enterica Serovar Typhimurium." Infection and Immunity 80, no. 9 (2012): 3289–96. http://dx.doi.org/10.1128/iai.00331-12.

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ABSTRACTSalmonella entericaserovar Typhimurium is a Gram-negative member of the familyEnterobacteriaceaeand is a common cause of bacterial food poisoning in humans. The fimbrial appendages are found on the surface of many enteric bacteria and enable the bacteria to bind to eukaryotic cells.S. Typhimurium type 1 fimbriae are characterized by mannose-sensitive hemagglutination and are assembled via the chaperone/usher pathway.S. Typhimurium type 1 fimbrial proteins are encoded by thefimgene cluster (fimAICDHFZYW), withfimAICDHFexpressed as a single transcriptional unit. The structural components

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2

Sebghati, Tricia A., and Steven Clegg. "Construction and Characterization of Mutations within theKlebsiella mrkD1P Gene That Affect Binding to Collagen Type V." Infection and Immunity 67, no. 4 (1999): 1672–76. http://dx.doi.org/10.1128/iai.67.4.1672-1676.1999.

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ABSTRACT The fimbria-associated MrkD1P protein mediates adherence of type 3 fimbriate strains of Klebsiella pneumoniae to collagen type V. Currently, three different MrkD adhesins have been described in Klebsiella species, and each possesses a distinctive binding pattern. Therefore, the binding abilities of mutants possessing defined mutations within themrkD 1P gene were examined in order to determine whether specific regions of the adhesin molecule were responsible for collagen binding. Both site-directed and chemically induced mutations were constructed within mrkD 1P, and the ability of the

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3

Zhang, Weiping, Ying Fang, and David H. Francis. "Characterization of the Binding Specificity of K88ac and K88ad Fimbriae of Enterotoxigenic Escherichia coli by Constructing K88ac/K88ad Chimeric FaeG Major Subunits." Infection and Immunity 77, no. 2 (2008): 699–706. http://dx.doi.org/10.1128/iai.01165-08.

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ABSTRACT Enterotoxigenic Escherichia coli (ETEC) strains expressing K88 (F4) fimbriae are the major cause of diarrhea in young pigs. Three antigenic variants of K88 fimbriae (K88ab, K88ac, and K88ad) have been identified among porcine ETEC strains. Each K88 fimbrial variant shows a unique pattern in binding to different receptors on porcine enterocytes. Such variant specificity in fimbrial binding is believed to be controlled by the major subunit (FaeG) of the K88 fimbriae, because the genes coding for the only other fimbrial subunit are identical among the three variants. Uniqueness in bindin

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Ray, Chad A., Linda E. Gfell, Tiffany L. Buller, and Richard L. Gregory. "Interactions of Streptococcus mutansFimbria-Associated Surface Proteins with Salivary Components." Clinical Diagnostic Laboratory Immunology 6, no. 3 (1999): 400–404. http://dx.doi.org/10.1128/cdli.6.3.400-404.1999.

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ABSTRACT Streptococcus mutans has been implicated as the major causative agent of human dental caries. S. mutans binds to saliva-coated tooth surfaces, and previous studies suggested that fimbriae may play a role in the initial bacterial adherence to salivary components. The objectives of this study were to establish the ability of an S. mutans fimbria preparation to bind to saliva-coated surfaces and determine the specific salivary components that facilitate binding with fimbriae. Enzyme-linked immunosorbent assay (ELISA) established that the S. mutans fimbria preparation bound to components

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5

Langstraat, Jennifer, Megan Bohse, and Steven Clegg. "Type 3 Fimbrial Shaft (MrkA) of Klebsiella pneumoniae, but Not the Fimbrial Adhesin (MrkD), Facilitates Biofilm Formation." Infection and Immunity 69, no. 9 (2001): 5805–12. http://dx.doi.org/10.1128/iai.69.9.5805-5812.2001.

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ABSTRACT Isolates of Klebsiella pneumoniae are responsible for opportunistic infections, particularly of the urinary tract and respiratory tract, in humans. These bacteria express type 3 fimbriae that have been implicated in binding to eucaryotic cells and matrix proteins. The type 3 fimbriae mediate binding to target tissue using the MrkD adhesin that is associated with the fimbrial shaft comprised of the MrkA protein. The formation of biofilms in vitro by strains ofK. pneumoniae was shown to be affected by the production of fimbriae on the bacterial surface. However, a functional MrkD adhesi

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Mishra, Arunima, Asis Das, John O. Cisar, and Hung Ton-That. "Sortase-Catalyzed Assembly of Distinct Heteromeric Fimbriae in Actinomyces naeslundii." Journal of Bacteriology 189, no. 8 (2007): 3156–65. http://dx.doi.org/10.1128/jb.01952-06.

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ABSTRACT Two types of adhesive fimbriae are expressed by Actinomyces; however, the architecture and the mechanism of assembly of these structures remain poorly understood. In this study we characterized two fimbrial gene clusters present in the genome of Actinomyces naeslundii strain MG-1. By using immunoelectron microscopy and biochemical analysis, we showed that the fimQ-fimP-srtC1-fimR gene cluster encodes a fimbrial structure (designated type 1) that contains a major subunit, FimP, forming the shaft and a minor subunit, FimQ, located primarily at the tip. Similarly, the fimB-fimA-srtC2 gen

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7

Virkola, Ritva, Mirko Brummer, Heikki Rauvala, Loek van Alphen, and Timo K. Korhonen. "Interaction of Fimbriae of Haemophilus influenzae Type B with Heparin-Binding Extracellular Matrix Proteins." Infection and Immunity 68, no. 10 (2000): 5696–701. http://dx.doi.org/10.1128/iai.68.10.5696-5701.2000.

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ABSTRACT The interaction of the fimbriae of Haemophilus influenzae type b (Hib) with two heparin-binding extracellular matrix proteins, human fibronectin (Fn) and heparin-binding growth-associated molecule (HB-GAM) from mouse, were studied. The fimbriated Hib strain 770235 fim+, as well as the recombinant strainE. coli HB101(pMH140), which expressed Hib fimbriae, adhered strongly to Fn and HB-GAM immobilized on glass. Purified Hib fimbriae bound to Fn and HB-GAM, and within the Fn molecule, the binding was localized to the N-terminal 30,000-molecular-weight (30K) and 40K fragments, which conta

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8

Altboum, Zeev, Myron M. Levine, James E. Galen, and Eileen M. Barry. "Genetic Characterization and Immunogenicity of Coli Surface Antigen 4 from Enterotoxigenic Escherichia coli when It Is Expressed in a Shigella Live-Vector Strain." Infection and Immunity 71, no. 3 (2003): 1352–60. http://dx.doi.org/10.1128/iai.71.3.1352-1360.2003.

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ABSTRACT The genes that encode the enterotoxigenic Escherichia coli (ETEC) CS4 fimbriae, csaA, -B, -C, -E, and -D′, were isolated from strain E11881A. The csa operon encodes a 17-kDa major fimbrial subunit (CsaB), a 40-kDa tip-associated protein (CsaE), a 27-kDa chaperone-like protein (CsaA), a 97-kDa usher-like protein (CsaC), and a deleted regulatory protein (CsaD′). The predicted amino acid sequences of the CS4 proteins are highly homologous to structural and assembly proteins of other ETEC fimbriae, including CS1 and CS2, and to CFA/I in particular. The csaA, -B, -C, -E operon was cloned o

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Pouttu, Riitta, Benita Westerlund-Wikström, Hannu Lång, et al. "matB, a Common Fimbrillin Gene ofEscherichia coli, Expressed in a Genetically Conserved, Virulent Clonal Group." Journal of Bacteriology 183, no. 16 (2001): 4727–36. http://dx.doi.org/10.1128/jb.183.16.4727-4736.2001.

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ABSTRACT A novel fimbrial type in Escherichia coli was identified and characterized. The expression of the fimbria was associated with the O18acK1H7 clonal group of E. coli, which cause newborn meningitis and septicemia when grown at low temperature; hence, it was named the Mat (meningitis associated and temperature regulated) fimbria. The fimbriae were purified from afimA::cat sfaA::GmfliC::St derivative of the O18K1H7 isolate E. coli IHE 3034. The purified Mat fimbrillin had an apparent molecular mass of 18 kDa and did not serologically cross-react with the type 1 or S fimbria of the same st

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10

Johnson, Jeremiah G., and Steven Clegg. "Role of MrkJ, a Phosphodiesterase, in Type 3 Fimbrial Expression and Biofilm Formation in Klebsiella pneumoniae." Journal of Bacteriology 192, no. 15 (2010): 3944–50. http://dx.doi.org/10.1128/jb.00304-10.

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ABSTRACT Klebsiella pneumoniae is an opportunistic pathogen that has been shown to adhere to human extracellular matrices using the type 3 fimbriae. Introduction of plasmids carrying genes known to alter intracellular cyclic-di-GMP pools in Vibrio parahaemolyticus revealed that these genes also altered type 3 fimbrial surface expression in K. pneumoniae. Immediately adjacent to the type 3 fimbrial gene cluster is a gene, mrkJ, that is related to a family of bacterial genes encoding phosphodiesterases. We identify here a role for MrkJ, a functional phosphodiesterase exhibiting homology to EAL d

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11

Hasegawa, Yoshiaki, Jun Iwami, Keiko Sato, et al. "Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae by the downstream gene product Mfa2." Microbiology 155, no. 10 (2009): 3333–47. http://dx.doi.org/10.1099/mic.0.028928-0.

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Porphyromonas gingivalis, a causative agent of periodontitis, has at least two types of thin, single-stranded fimbriae, termed FimA and Mfa1 (according to the names of major subunits), which can be discriminated by filament length and by the size of their major fimbrilin subunits. FimA fimbriae are long filaments that are easily detached from cells, whereas Mfa1 fimbriae are short filaments that are tightly bound to cells. However, a P. gingivalis ATCC 33277-derived mutant deficient in mfa2, a gene downstream of mfa1, produced long filaments (10 times longer than those of the parent), easily d

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Kuan, Lisa, Jessica N. Schaffer, Christos D. Zouzias, and Melanie M. Pearson. "Characterization of 17 chaperone-usher fimbriae encoded by Proteus mirabilis reveals strong conservation." Journal of Medical Microbiology 63, no. 7 (2014): 911–22. http://dx.doi.org/10.1099/jmm.0.069971-0.

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Proteus mirabilis is a Gram-negative enteric bacterium that causes complicated urinary tract infections, particularly in patients with indwelling catheters. Sequencing of clinical isolate P. mirabilis HI4320 revealed the presence of 17 predicted chaperone-usher fimbrial operons. We classified these fimbriae into three groups by their genetic relationship to other chaperone-usher fimbriae. Sixteen of these fimbriae are encoded by all seven currently sequenced P. mirabilis genomes. The predicted protein sequence of the major structural subunit for 14 of these fimbriae was highly conserved (≥95 %

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Jagnow, Jennifer, and Steven Clegg. "Klebsiella pneumoniae MrkD-mediated biofilm formation on extracellular matrix- and collagen-coated surfaces." Microbiology 149, no. 9 (2003): 2397–405. http://dx.doi.org/10.1099/mic.0.26434-0.

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The type 3 fimbriae of Klebsiella pneumoniae are comprised of the major fimbrial subunit (MrkA) and the adhesin (MrkD) that has previously been shown to mediate binding to collagen. The ability of adhesive and non-adhesive derivatives of K. pneumoniae to form biofilms on collagen-coated surfaces in continuous-flow chambers was investigated. Unlike biofilm formation on abiotic plastic surfaces, the presence of the MrkD adhesin was necessary for growth on collagen-coated surfaces. Fimbriate strains lacking the MrkD adhesin did not efficiently adhere to and grow on these surfaces. Similarly, puri

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14

Hacker, Jörg. "Role of fimbrial adhesins in the pathogenesis of Escherichia coli infections." Canadian Journal of Microbiology 38, no. 7 (1992): 720–27. http://dx.doi.org/10.1139/m92-118.

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Escherichia coli strains are able to cause intestinal (enteritis, diarrhoeal diseases) and extraintestinal (urinary tract infections, sepsis, meningitis) infections. Most pathogenic E. coli strains produce specific fimbrial adhesins, which represent essential colonization factors: intestinal E. coli strains very often carry transferable plasmids with gene clusters specific for fimbrial adhesins, like K88 and K99, or colonization factor antigens (CFA) I and II. In contrast, the fimbrial gene clusters of extraintestinal E. coli strains, such as P, S, or F1C fimbriae, are located on the chromosom

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Anantha, Ravi P., Annette L. McVeigh, Lanfong H. Lee, et al. "Evolutionary and Functional Relationships of Colonization Factor Antigen I and Other Class 5 Adhesive Fimbriae of Enterotoxigenic Escherichia coli." Infection and Immunity 72, no. 12 (2004): 7190–201. http://dx.doi.org/10.1128/iai.72.12.7190-7201.2004.

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ABSTRACT Colonization factor antigen I (CFA/I) is the archetype of eight genetically related fimbriae of enterotoxigenic Escherichia coli (ETEC) designated class 5 fimbriae. Assembled by the alternate chaperone pathway, these organelles comprise a rigid stalk of polymerized major subunits and an apparently tip-localized minor adhesive subunit. We examined the evolutionary relationships of class 5-specific structural proteins and correlated these with functional properties. We sequenced the gene clusters encoding coli surface antigen 4 (CS4), CS14, CS17, CS19, and putative colonization factor a

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Castle, Alan J., Robert Boulianne, Jianhua Xu, and Alan W. Day. "Posttranslational modification of fimbrial protein from Ustilago violacea." Canadian Journal of Microbiology 38, no. 11 (1992): 1144–49. http://dx.doi.org/10.1139/m92-187.

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Fimbriae from the fungus Ustilago violacea were shown to consist of 74-kDa protein subunits. The 74-kDa protein was strongly recognized on immunoblots reacted with a polyclonal antiserum against U. violacea fimbrial protein. Staining of the subunits with periodic acid – Schiff reagent indicated that the proteins were glycosylated. Approximately 10% of the glycoprotein was estimated to be carbohydrate, since treatment of defimbriated cells with tunicamycin or removal of the carbohydrate portion of the subunit by trifluoromethanesulfonic acid treatment resulted in a 67-kDa polypeptide. Mannose w

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Balsalobre, Carlos, Joachim Morschhäuser, Jana Jass, Jörg Hacker, and Bernt Eric Uhlin. "Transcriptional Analysis of the sfa Determinant Revealing Multiple mRNA Processing Events in the Biogenesis of S Fimbriae in Pathogenic Escherichia coli." Journal of Bacteriology 185, no. 2 (2003): 620–29. http://dx.doi.org/10.1128/jb.185.2.620-629.2003.

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ABSTRACT Among the virulence factors present in pathogenic extraintestinal Escherichia coli strains, expression of fimbrial adhesins is necessary for attachment to the host tissues and subsequent colonization. Occurrence of the sfa determinant coding for the S fimbriae is widespread among the uropathogens and meningitis isolates. The sfa operon consists of nine genes. In the biogenesis of S fimbriae, the proteins encoded by the sfa genes are presumably required in a specific stoichiometry. In the present work we studied how differential expression of the sfa operon genes occurs. Our findings i

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Pierce, Deanne L., So-ichiro Nishiyama, Shuang Liang, et al. "Host Adhesive Activities and Virulence of Novel Fimbrial Proteins of Porphyromonas gingivalis." Infection and Immunity 77, no. 8 (2009): 3294–301. http://dx.doi.org/10.1128/iai.00262-09.

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ABSTRACT The fimbriae of Porphyromonas gingivalis mediate critical roles in host colonization and evasion of innate defenses and comprise polymerized fimbrilin (FimA) associated with quantitatively minor accessory proteins (FimCDE) of unknown function. We now show that P. gingivalis fimbriae lacking FimCDE fail to interact with the CXC-chemokine receptor 4 (CXCR4), and bacteria expressing FimCDE-deficient fimbriae cannot exploit CXCR4 in vivo for promoting their persistence, as the wild-type organism does. Consistent with these loss-of-function experiments, purified FimC and FimD (but not FimE

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Farfan, Mauricio J., Lidia Cantero, Roberto Vidal, Douglas J. Botkin, and Alfredo G. Torres. "Long Polar Fimbriae of Enterohemorrhagic Escherichia coli O157:H7 Bind to Extracellular Matrix Proteins." Infection and Immunity 79, no. 9 (2011): 3744–50. http://dx.doi.org/10.1128/iai.05317-11.

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ABSTRACTAdherence to intestinal cells is a key process in infection caused by enterohemorrhagicEscherichia coli(EHEC). Several adhesion factors that mediate the binding of EHEC to intestinal cells have been described, but the receptors involved in their recognition are not fully characterized. Extracellular matrix (ECM) proteins might act as receptors involved in the recognition of enteric pathogens, including EHEC. In this study, we sought to characterize the binding of EHEC O157:H7 to ECM proteins commonly present in the intestine. We found that EHEC prototype strains as well as other clinic

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Ledeboer, Nathan A., Jonathan G. Frye, Michael McClelland, and Bradley D. Jones. "Salmonella enterica Serovar Typhimurium Requires the Lpf, Pef, and Tafi Fimbriae for Biofilm Formation on HEp-2 Tissue Culture Cells and Chicken Intestinal Epithelium." Infection and Immunity 74, no. 6 (2006): 3156–69. http://dx.doi.org/10.1128/iai.01428-05.

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ABSTRACT Recent work has demonstrated that Salmonella enterica serovar Typhimurium forms biofilms on HEp-2 tissue culture cells in a type 1 fimbria-dependent manner. To investigate how biofilm growth of HEp-2 tissue culture cells affects gene expression in Salmonella, we compared global gene expression during planktonic growth and biofilm growth. Microarray results indicated that the transcription of ∼100 genes was substantially altered by growth in a biofilm. These genes encode proteins with a wide range of functions, including antibiotic resistance, central metabolism, conjugation, intracell

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Mahon, Vivienne, Cyril J. Smyth, and Stephen G. J. Smith. "Mutagenesis of the Rns regulator of enterotoxigenic Escherichia coli reveals roles for a linker sequence and two helix–turn–helix motifs." Microbiology 156, no. 9 (2010): 2796–806. http://dx.doi.org/10.1099/mic.0.038521-0.

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The pathogenesis of diarrhoeal disease due to human enterotoxigenic Escherichia coli absolutely requires the expression of fimbriae. The expression of CS1 fimbriae is positively regulated by the AraC-like protein Rns. AraC-like proteins are DNA-binding proteins that typically contain two helix–turn–helix (HTH) motifs. A program of pentapeptide insertion mutagenesis of the Rns protein was performed, and this revealed that both HTH motifs are required by Rns to positively regulate CS1 fimbrial gene expression. Intriguingly, a pentapeptide insertion after amino acid C102 reduced the ability of Rn

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Nicholson, Tracy L., and Andreas J. Bäumler. "Salmonella enterica Serotype Typhimurium Elicits Cross-Immunity against a Salmonella enterica Serotype Enteritidis Strain Expressing LP Fimbriae from thelac Promoter." Infection and Immunity 69, no. 1 (2001): 204–12. http://dx.doi.org/10.1128/iai.69.1.204-212.2001.

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ABSTRACT The biological significance of fimbrial phase variation inSalmonella serotypes is currently unknown. Exposure to long polar (LP) fimbriae of Salmonella enterica serotype Typhimurium results in selection against lpf phase ON cells of serotype Enteritidis during a subsequent challenge, suggesting that fimbrial phase variation may be a mechanism to evade cross-immunity between Salmonella serotypes. This notion was tested by assessing the effect of an immune response against serotype Typhimurium LP fimbriae on colonization of mice with a serotype Enteritidis mutant in which the lpf promot

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Pearce, A. M., L. I. Irons, A. Robinson, and R. N. Seabrook. "Effects of guanidinium hydrochloride on the structure and immunological properties of Bordetella pertussis fimbriae." Biochemical Journal 283, no. 3 (1992): 823–28. http://dx.doi.org/10.1042/bj2830823.

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Denaturation of Bordetella pertussis fimbrial preparations by guanidinium hydrochloride (GdnHCl) has been characterized using static light scattering, c.d., fluorescence and antibody recognition. The susceptibility of Fim2 + 3 (a mixed preparation of two fimbrial types) to GdnHCl was found to be highly dependent on pH; as the pH was increased from pH 7.2 to 10.5, the concentration of GdnHCl required to induce 50% denaturation was decreased. At pH 10.5, Fim2 + 3 was denatured by GdnHCl in a three-step pathway comprising: (1) formation of a pre-denaturational intermediate at less than 1.0 M-GdnH

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Amano, Atsuo, Takayuki Nakamura, Shigenobu Kimura, et al. "Molecular Interactions of Porphyromonas gingivalisFimbriae with Host Proteins: Kinetic Analyses Based on Surface Plasmon Resonance." Infection and Immunity 67, no. 5 (1999): 2399–405. http://dx.doi.org/10.1128/iai.67.5.2399-2405.1999.

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ABSTRACT Fimbriae of Porphyromonas gingivalis are thought to play an important role in the colonization and invasion of periodontal tissues. In this study, we analyzed the interactions of P. gingivalis fimbriae with human hemoglobin, fibrinogen, and salivary components (i.e., proline-rich protein [PRP], proline-rich glycoprotein [PRG], and statherin) based on surface plasmon resonance (SPR) spectroscopy with a biomolecular interaction analyzing system (BIAcore). The real-time observation showed that the fimbriae interacted more quickly with hemoglobin and PRG than with other proteins and more

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Fang, Lin, Zhibo Gan, and Ronald R. Marquardt. "Isolation, Affinity Purification, and Identification of Piglet Small Intestine Mucosa Receptor for Enterotoxigenic Escherichia coli K88ac+ Fimbriae." Infection and Immunity 68, no. 2 (2000): 564–69. http://dx.doi.org/10.1128/iai.68.2.564-569.2000.

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ABSTRACT An affinity chromatography technique was utilized to isolate and purify the receptors of Escherichia coli K88ac+fimbriae from the mucus of the small intestines of newborn piglets. Purified K88ac+ fimbriae were covalently immobilized onto a beaded agarose matrix (Sepharose 4B). The immobilized fimbriae were used for the affinity purification of the K88ac+ receptors. Only two major proteins were tightly and specifically bound to the immobilized fimbriae after the column containing bound receptor was washed exhaustively with a buffer containing a high concentration of salt and a detergen

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Celerin, Martina, Alan W. Day, Ronald J. Smith, and David E. Laudenbach. "Immunolocalization of fimbrial epitopes in thin sections of Microbotryum violaceum." Canadian Journal of Microbiology 43, no. 2 (1997): 136–42. http://dx.doi.org/10.1139/m97-018.

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Fungal fimbriae are long (0.5–20 μm), narrow (7 nm) surface appendages that have been observed on most members of the Mycota. Biochemical analyses have determined that fimbriae from Microbotryum violaceum are composed of 74-kDa glycoproteinaceous subunits in which the protein moiety is fungal collagen. We present evidence for the localization of fimbrial subunits prior to their exportation from the cell. We term these internal, likely nonpolymerized fimbriae "pro-fimbriae" and demonstrate the location of the reserves within the peripheral cytoplasm. Also, we show that fimbriae may not traverse

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Bao, Rui, Lothar Esser, Steven Poole, et al. "Preliminary X-ray diffraction analysis of CfaA, a molecular chaperone essential for the assembly of CFA/I fimbriae of human enterotoxigenicEscherichia coli." Acta Crystallographica Section F Structural Biology Communications 70, no. 2 (2014): 196–99. http://dx.doi.org/10.1107/s2053230x13033967.

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Understanding of pilus bioassembly in Gram-negative bacteria stems mainly from studies of P pili and type 1 fimbriae of uropathogenicEscherichia coli, which are mediated by the classic chaperone–usher pathway (CUP). However, CFA/I fimbriae, a class 5 fimbria and intestinal colonization factor for enterotoxigenicE. coli(ETEC), are proposed to assembleviathe alternate chaperone pathway (ACP). Both CUP and ACP fimbrial bioassembly pathways require the function of a periplasmic chaperone, but their corresponding proteins share very low similarity in primary sequence. Here, the crystallization of t

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Sojar, Hakimuddin T., Ashu Sharma, and Robert J. Genco. "Porphyromonas gingivalis Fimbriae Bind to Cytokeratin of Epithelial Cells." Infection and Immunity 70, no. 1 (2002): 96–101. http://dx.doi.org/10.1128/iai.70.1.96-101.2002.

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ABSTRACT The adherence of Porphyromonas gingivalis to host cells is likely a prerequisite step in the pathogenesis of P. gingivalis-induced periodontal disease. P. gingivalis binds to and invades epithelial cells, and fimbriae are shown to be involved in this process. Little is known regarding epithelial receptor(s) involved in binding of P. gingivalis fimbriae. Using an overlay assay with purified P. gingivalis fimbriae as a probe, two major epithelial cell proteins with masses of 50 and 40 kDa were identified by immunoblotting with fimbria-specific antibodies. Iodinated purified fimbriae als

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Smeds, A., M. Pertovaara, T. Timonen, T. Pohjanvirta, S. Pelkonen, and A. Palva. "Mapping the Binding Domain of the F18 Fimbrial Adhesin." Infection and Immunity 71, no. 4 (2003): 2163–72. http://dx.doi.org/10.1128/iai.71.4.2163-2182.2003.

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ABSTRACT F18 fimbrial Esherichia coli strains are associated with porcine postweaning diarrhea and pig edema disease. Recently, the FedF subunit was identified as the adhesin of the F18 fimbriae. In this study, adhesion domains of FedF were further studied by constructing deletions within the fedF gene and expressing FedF proteins with deletions either together with the other F18 fimbrial subunits or as fusion proteins tagged with maltose binding protein. The region essential for adhesion to porcine intestinal epithelial cells was mapped between amino acid residues 60 and 109 of FedF. To map t

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Izquierdo, Mariana, Fernando Navarro-Garcia, Raul Nava-Acosta, James P. Nataro, Fernando Ruiz-Perez, and Mauricio J. Farfan. "Identification of Cell Surface-Exposed Proteins Involved in the Fimbria-Mediated Adherence of Enteroaggregative Escherichia coli to Intestinal Cells." Infection and Immunity 82, no. 4 (2014): 1719–24. http://dx.doi.org/10.1128/iai.01651-13.

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ABSTRACTFimbria-mediated adherence to the intestinal epithelia is a key step in enteroaggregativeEscherichia coli(EAEC) pathogenesis. To date, four fimbriae have been described for EAEC; aggregative adherence fimbria II (AAF/II) is the most important adherence factor for EAEC prototype strain 042. Previously, we described results showing that extracellular matrix (ECM) components might be involved in the recognition of AAF/II fimbriae by intestinal cells. In this study, we sought to identify novel potential receptors on intestinal epithelial cells recognized by the AAF/II fimbriae. Purified Aa

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Sakae, Kotaro, Keiji Nagano, Miyuna Furuhashi, and Yoshiaki Hasegawa. "Diversity analysis of genes encoding Mfa1 fimbrial components in Porphyromonas gingivalis strains." PLOS ONE 16, no. 7 (2021): e0255111. http://dx.doi.org/10.1371/journal.pone.0255111.

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Porphyromonas gingivalis, a gram-negative anaerobic bacterium, is associated with the development of periodontal disease. The genetic diversity in virulence factors, such as adhesive fimbriae, among its strains affects the bacterial pathogenicity. P. gingivalis generally expresses two distinct types of fimbriae, FimA and Mfa1. Although the genetic diversity of fimA, encoding the major FimA fimbrilin protein, has been characterized, the genes encoding the Mfa1 fimbrial components, including the Mfa1 to Mfa5 proteins, have not been fully studied. We, therefore, analyzed their genotypes in 12 unc

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Parker, Dane, Ruth M. Kennan, Garry S. Myers, Ian T. Paulsen, J. Glenn Songer, and Julian I. Rood. "Regulation of Type IV Fimbrial Biogenesis in Dichelobacter nodosus." Journal of Bacteriology 188, no. 13 (2006): 4801–11. http://dx.doi.org/10.1128/jb.00255-06.

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ABSTRACT Type IV fimbriae are expressed by several bacterial pathogens and are essential for virulence in Dichelobacter nodosus, which causes ovine footrot. We have identified a two-component signal transduction system (PilR/S) and an alternative sigma factor (σ54) that were shown by insertional inactivation to be required for the regulation of fimbrial biogenesis in D. nodosus. Western blots showed that in both pilR and rpoN mutants, fimbrial subunit production was significantly reduced by a process that was shown to occur at a PilR- and σ54-dependent promoter. The mutants lacked surface fimb

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Han, Xiaoyan, Ruth M. Kennan, Dane Parker, John K. Davies, and Julian I. Rood. "Type IV Fimbrial Biogenesis Is Required for Protease Secretion and Natural Transformation in Dichelobacter nodosus." Journal of Bacteriology 189, no. 14 (2007): 5022–33. http://dx.doi.org/10.1128/jb.00138-07.

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ABSTRACT The objective of this study was to develop an understanding of the molecular mechanisms by which type IV fimbrial biogenesis, natural transformation, and protease secretion are linked in the ovine foot rot pathogen, Dichelobacter nodosus. We have shown that like the D. nodosus fimbrial subunit FimA, the pilin-like protein PilE and the FimN, FimO, and FimP proteins, which are homologs of PilB, PilC, and PilD from Pseudomonas aeruginosa, are essential for fimbrial biogenesis and natural transformation, indicating that transformation requires an intact type IV fimbrial apparatus. The res

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Van Loy, Cristina P., Evgeni V. Sokurenko, and Steve L. Moseley. "The Major Structural Subunits of Dr and F1845 Fimbriae Are Adhesins." Infection and Immunity 70, no. 4 (2002): 1694–702. http://dx.doi.org/10.1128/iai.70.4.1694-1702.2002.

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ABSTRACT Fimbrial adhesins mediate the attachment of pathogenic Escherichia coli to various host tissues leading to the development of disease. The Dr hemagglutinin and F1845 fimbriae belong to the Dr family of adhesins, which is associated with urinary tract infections and diarrheal disease. These adhesins bind to the Dra blood-group antigen present on decay-accelerating factor (DAF). The Dr hemagglutinin is unique in this family since it also binds to type IV collagen and its binding is inhibited by the presence of chloramphenicol. We have purified the major structural subunits of Dr and F18

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Zalewska-Piątek, Beata, Katarzyna Bury, Rafał Piątek, Piotr Bruździak, and Józef Kur. "Type II Secretory Pathway for Surface Secretion of DraD Invasin from the Uropathogenic Escherichia coli Dr+ Strain." Journal of Bacteriology 190, no. 14 (2008): 5044–56. http://dx.doi.org/10.1128/jb.00224-08.

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ABSTRACT The virulence of the uropathogenic Escherichia coli Dr+ IH11128 strain is associated with the presence of Dr fimbrial structures and a DraD invasin which can act as a fimbrial capping domain at the bacterial cell surface. However, a recent study suggests that the DraD protein is surface exposed in two forms: fimbria associated and fimbria nonassociated (prone to interaction with the N-terminal extension of the DraE protein located on the fimbrial tip). The actual mechanism of DraD surface secretion is presently unknown. We identified a previously unrecognized type II secretory pathway

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Park, Yoonsuk, M. Regina Simionato, Kachiko Sekiya, et al. "Short Fimbriae of Porphyromonas gingivalis and Their Role in Coadhesion with Streptococcus gordonii." Infection and Immunity 73, no. 7 (2005): 3983–89. http://dx.doi.org/10.1128/iai.73.7.3983-3989.2005.

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ABSTRACT Porphyromonas gingivalis, one of the causative agents of adult periodontitis, attaches and forms biofilms on substrata of Streptococcus gordonii. Coadhesion and biofilm development between these organisms requires the interaction of the short fimbriae of P. gingivalis with the SspB streptococcal surface polypeptide. In this study we investigated the structure and binding activities of the short fimbriae of P. gingivalis. Electron microscopy showed that isolated short fimbriae have an average length of 103 nm and exhibit a helical structure with a pitch of ca. 27 nm. Mfa1, the major pr

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Haase, Elaine M., Joyce L. Zmuda, and Frank A. Scannapieco. "Identification and Molecular Analysis of Rough-Colony-Specific Outer Membrane Proteins of Actinobacillus actinomycetemcomitans." Infection and Immunity 67, no. 6 (1999): 2901–8. http://dx.doi.org/10.1128/iai.67.6.2901-2908.1999.

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ABSTRACT Actinobacillus actinomycetemcomitans, a gram-negative bacterium isolated from the human mouth, has been implicated in the pathogenesis of early-onset periodontitis. Primary isolates cultured from subgingival plaque exhibit an adherent, rough colony phenotype which spontaneously converts to a nonadherent, smooth phenotype upon in vitro subculture. The rough colony variant produces abundant fimbriae and autoaggregates, while the smooth colony variant is planktonic and produces scant fimbriae. To begin to understand the significance of colony variation in biofilm formation by A. actinomy

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Masuda, Takashi, Yukitaka Murakami, Toshihide Noguchi, and Fuminobu Yoshimura. "Effects of Various Growth Conditions in a Chemostat on Expression of Virulence Factors in Porphyromonas gingivalis." Applied and Environmental Microbiology 72, no. 5 (2006): 3458–67. http://dx.doi.org/10.1128/aem.72.5.3458-3467.2006.

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ABSTRACT Porphyromonas gingivalis, one of the gram-negative organisms associated with periodontal disease, possesses potential virulence factors, including fimbriae, proteases, and major outer membrane proteins (OMPs). In this study, P. gingivalis ATCC 33277 was cultured in a chemostat under hemin excess and presumably peptide-limiting conditions to better understand the mechanisms of expression of the virulence factors upon environmental changes. At higher growth rates, the amounts of FimA and the 75-kDa protein, forming long and short fimbriae, respectively, increased significantly, whereas

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Grzymajło, Krzysztof, Marta Kuźmińska-Bajor, Jakub Jaworski, Piotr Dobryszycki, and Maciej Ugorski. "The high-adhesive properties of the FimH adhesin of Salmonella enterica serovar Enteritidis are determined by a single F118S substitution." Microbiology 156, no. 6 (2010): 1738–48. http://dx.doi.org/10.1099/mic.0.039206-0.

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The binding properties of low- and high-adhesive forms of FimH adhesins from Salmonella enterica serovars Enteritidis and Typhimurium (S. Enteritidis and S. Typhimurium) were studied using chimeric proteins containing an additional peptide that represents an N-terminal extension of the FimF protein. This modification, by taking advantage of a donor strand exchange mechanism, closes the hydrophobic groove in the fimbrial domain of the FimH adhesin. Such self-complemented adhesins (scFimH) did not form aggregates and were more stable (resistant to proteolytic cleavage) than native FimH. High-adh

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Gousset, Nathalie, Agnes Rosenau, Pierre-Yves Sizaret, and Roland Quentin. "Nucleotide Sequences of Genes Coding for Fimbrial Proteins in a Cryptic Genospecies of Haemophilus spp. Isolated from Neonatal and Genital Tract Infections." Infection and Immunity 67, no. 1 (1999): 8–15. http://dx.doi.org/10.1128/iai.67.1.8-15.1999.

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ABSTRACT Nineteen isolates belonging to a cryptic genospecies ofHaemophilus (referred to here as genital strains) isolated from genital tract infections (6 strains) and from neonatal infections (13 strains) were studied for fimbrial genes. Sixteen strains exhibit peritrichous fimbriae observed by electron microscopy. By PCR with primers corresponding to the extreme ends of the Haemophilus influenzae type b (Hib) hifA and hifDgenes and Southern blotting, a hifA-like gene (namedghfA) and a hifD-like gene (namedghfD) were identified in 6 of the 19 strains. Five of these six strains were from the

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Rani, D. B. Rajini, Manfred E. Bayer, and Dieter M. Schifferli. "Polymeric Display of Immunogenic Epitopes from Herpes Simplex Virus and Transmissible Gastroenteritis Virus Surface Proteins on an Enteroadherent Fimbria." Clinical Diagnostic Laboratory Immunology 6, no. 1 (1999): 30–40. http://dx.doi.org/10.1128/cdli.6.1.30-40.1999.

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ABSTRACT The strong immunogenicity of bacterial fimbriae results from their polymeric and proteinaceous nature, and the protective role of these immunogens in experimental or commercial vaccines is associated with their capacity to induce antiadhesive antibodies. Fimbria-mediated intestinal colonization by enteropathogens typically leads to similar antibody responses. The possibility of taking advantage of these properties was investigated by determining whether enteroadhesive fimbriae, like the 987P fimbriae of enterotoxigenic Escherichia coli, can serve as carriers for foreign antigens witho

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Bode, Nadine J., Kun-Wei Chan, Xiang-Peng Kong, and Melanie M. Pearson. "Distinct Residues Contribute to Motility Repression and Autoregulation in the Proteus mirabilis Fimbria-Associated Transcriptional Regulator AtfJ." Journal of Bacteriology 198, no. 15 (2016): 2100–2112. http://dx.doi.org/10.1128/jb.00193-16.

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ABSTRACTProteus mirabiliscontributes to a significant number of catheter-associated urinary tract infections, where coordinated regulation of adherence and motility is critical for ascending disease progression. Previously, the mannose-resistantProteus-like (MR/P) fimbria-associated transcriptional regulator MrpJ has been shown to both repress motility and directly induce the transcription of its own operon; in addition, it affects the expression of a wide range of cellular processes. Interestingly, 14 additionalmrpJparalogs are included in theP. mirabilisgenome. Looking at a selection of MrpJ

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Geuijen, Cecile A. W., Rob J. L. Willems, Peter Hoogerhout, Wouter C. Puijk, Rob H. Meloen, and Frits R. Mooi. "Identification and Characterization of Heparin Binding Regions of the Fim2 Subunit of Bordetella pertussis." Infection and Immunity 66, no. 5 (1998): 2256–63. http://dx.doi.org/10.1128/iai.66.5.2256-2263.1998.

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ABSTRACT Bordetella pertussis fimbriae bind to sulfated sugars such as heparin through the major subunit Fim2. The Fim2 subunit contains two regions, designated H1 and H2, which show sequence similarity with heparin binding regions of fibronectin, and the role of these regions in heparin binding was investigated with maltose binding protein (MBP)-Fim2 fusion proteins. Deletion derivatives of MBP-Fim2 showed that both regions are important for binding to heparin. The role of H2 in heparin binding was confirmed by site-directed mutagenesis in which basic amino acids were replaced by alanine. The

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Day, A. W., R. B. Gardiner, R. Smith, A. M. Svircev, and W. E. McKeen. "Detection of fungal fimbriae by protein A – gold immunocytochemical labelling in host plants infected with Ustilago heufleri or Peronospora hyoscyami f.sp. tabacina." Canadian Journal of Microbiology 32, no. 7 (1986): 577–84. http://dx.doi.org/10.1139/m86-107.

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Sections of leaves of Nicotiana tabacum L. infected with Peronospora hyoscyami De Bary f.sp. tabacina (Adam) Skalicky and of Erythronium americanum Ker. infected with Ustilago heufleri Fuckel were treated with an antiserum directed against the fimbriae of U. violacea Fuckel and other fungi. The sections were then treated with protein A – gold complexes to detect the presence and location of fimbrial antigens following transmission or scanning electron microscopy. Control preparations involved sections of uninfected leaves, as well as a range of serological control treatments. The infected leaf

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Johnston, Joanne L., Stephen J. Billington, Volker Haring, and Julian I. Rood. "Complementation Analysis of the Dichelobacter nodosus fimN, fimO, and fimP Genes inPseudomonas aeruginosa and Transcriptional Analysis of thefimNOP Gene Region." Infection and Immunity 66, no. 1 (1998): 297–304. http://dx.doi.org/10.1128/iai.66.1.297-304.1998.

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ABSTRACT The causative agent of ovine footrot, the gram-negative anaerobeDichelobacter nodosus, produces polar type IV fimbriae, which are the major protective antigens. The D. nodosusgenes fimN, fimO, and fimP are homologs of the Pseudomonas aeruginosa fimbrial assembly genes, pilB, pilC, and pilD, respectively. Both the pilD and fimP genes encode prepilin peptidases that are responsible for cleavage of the leader sequence from the immature fimbrial subunit. To investigate the functional similarity of the fimbrial biogenesis systems from these organisms, the D. nodosus genes were introduced i

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Chung, Whasun O., Donald R. Demuth, and Richard J. Lamont. "Identification of a Porphyromonas gingivalis Receptor for the Streptococcus gordoniiSspB Protein." Infection and Immunity 68, no. 12 (2000): 6758–62. http://dx.doi.org/10.1128/iai.68.12.6758-6762.2000.

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ABSTRACT Colonization of the plaque biofilm by the oral pathogenPorphyromonas gingivalis is favored by the presence of antecedent organisms such as Streptococcus gordonii. Coadhesion between P. gingivalis and S. gordonii can be mediated by the SspB protein of S. gordonii; however, the P. gingivalis cognate receptor for this protein has not been identified. In this study, we identified a surface protein of P. gingivalis that interacts with the SspB protein. Coprecipitation between P. gingivalis outer membrane proteins and purified SspB protein demonstrated that a 100-kDaP. gingivalis protein bo

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Fontana, Margherita, Ann J. Dunipace, George K. Stookey, and Richard L. Gregory. "Intranasal Immunization against Dental Caries with a Streptococcus mutans-Enriched Fimbrial Preparation." Clinical Diagnostic Laboratory Immunology 6, no. 3 (1999): 405–9. http://dx.doi.org/10.1128/cdli.6.3.405-409.1999.

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ABSTRACT Streptococcus mutans has been identified as the major etiological agent of human dental caries. The first step in the initiation of infection by this pathogenic bacterium is its attachment (i.e., through bacterial surface proteins such as glucosyltransferases, P1, glucan-binding proteins, and fimbriae) to a suitable receptor. It is hypothesized that a mucosal vaccine against a combination ofS. mutans surface proteins would protect against dental caries by inducing specific salivary immunoglobulin A (IgA) antibodies which may reduce bacterial pathogenesis and adhesion to the tooth surf

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Siegel, Sara D., Chenggang Wu, and Hung Ton-That. "A Type I Signal Peptidase Is Required for Pilus Assembly in the Gram-Positive, Biofilm-Forming Bacterium Actinomycesoris." Journal of Bacteriology 198, no. 15 (2016): 2064–73. http://dx.doi.org/10.1128/jb.00353-16.

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ABSTRACTThe Gram-positive bacteriumActinomycesoris, a key colonizer in the development of oral biofilms, contains 18 LPXTG motif-containing proteins, including fimbrillins that constitute two fimbrial types critical for adherence, biofilm formation, and polymicrobial interactions. Export of these protein precursors, which harbor a signal peptide, is thought to be mediated by the Sec machine and require cleavage of the signal peptide by type I signal peptidases (SPases). Like many Gram-positive bacteria,A. orisexpresses two SPases, named LepB1 and LepB2. The latter has been linked to suppressio

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Tinker, Juliette K., and Steven Clegg. "Characterization of FimY as a Coactivator of Type 1 Fimbrial Expression in Salmonella enterica Serovar Typhimurium." Infection and Immunity 68, no. 6 (2000): 3305–13. http://dx.doi.org/10.1128/iai.68.6.3305-3313.2000.

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ABSTRACT Type 1 fimbriae of Salmonella enterica serovar Typhimurium are surface appendages that carry adhesins specific for mannosylated host glycoconjugates. Regulation of the major fimbrial subunit is thought to be controlled by a number of ancillaryfim genes, including fimZ, fimY,fimW, and fimU. Previous studies using a FimZ mutant have indicated that this protein is necessary forfimA expression, and in vitro DNA binding assays determined that FimZ is a transcriptional activator that binds directly to thefimA promoter. To determine the role of FimY as a potential regulator of fimbrial expre

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Stubenrauch, Christopher J., Gordon Dougan, Trevor Lithgow, and Eva Heinz. "Constraints on lateral gene transfer in promoting fimbrial usher protein diversity and function." Open Biology 7, no. 11 (2017): 170144. http://dx.doi.org/10.1098/rsob.170144.

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Fimbriae are long, adhesive structures widespread throughout members of the family Enterobacteriaceae. They are multimeric extrusions, which are moved out of the bacterial cell through an integral outer membrane protein called usher. The complex folding mechanics of the usher protein were recently revealed to be catalysed by the membrane-embedded translocation and assembly module (TAM). Here, we examine the diversity of usher proteins across a wide range of extraintestinal (ExPEC) and enteropathogenic (EPEC) Escherichia coli , and further focus on a so far undescribed chaperone–usher system, w

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