نتایج جستجو برای: filamentous hemagglutinin

تعداد نتایج: 27081  

2013
Hossein Asgarian-Omran Ali Akbar Amirzargar Mohammad Arjmand Mohammadreza Eshraghian Behrooz Nikbin Saeid Eshraghi Marzieh Mahdavi Jalal Khoshnoodi Mahmood Jeddi-Tehrani Hodjatallah Rabbani Fazel Shokri

BACKGROUND Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. METHODS Three overlapping coding sequences ...

2015
Erich V. Scheller Jeffrey A. Melvin Amanda J. Sheets Peggy A. Cotter

UNLABELLED Bordetella fimbriae (FIM) are generally considered to function as adhesins despite a lack of experimental evidence supporting this conclusion for Bordetella pertussis and evidence against a requirement for FIM in adherence of Bordetella bronchiseptica to mammalian cell lines. Using B. bronchiseptica and mice, we developed an in vivo adherence assay that revealed that FIM do function ...

Journal: :Infection and immunity 1990
A M Delisse-Gathoye C Locht F Jacob M Raaschou-Nielsen I Heron J L Ruelle M de Wilde T Cabezon

The gene coding for the filamentous hemagglutinin (FHA), one of the main factors involved in mediating adherence of Bordetella pertussis to ciliated host cells, was cloned in Escherichia coli, and the 3,500-base-pair nucleotide sequence encoding the amino-terminal region was determined. Molecular cloning, together with the characterization of recombinant FHA-related proteins produced in E. coli...

Journal: :Infection and immunity 2007
Pascale Plamondon Nicole R Luke Anthony A Campagnari

Although Moraxella catarrhalis continues to be a significant cause of disease in both children and adults, the steps involved in pathogenesis remain poorly understood. We have identified three open reading frames in the M. catarrhalis genome that encode homologues of the two-partner secretion system (TPS). The sequenced M. catarrhalis hemagglutinin-like locus of strain 7169 has a unique gene or...

Journal: :Infection and immunity 1991
Y L Zhang R D Sekura

A procedure is described for purification of pertussis heat-labile toxin (PEHLT) from cells of Bordetella pertussis. The purification procedure, performed in the cold and in the presence of protease inhibitors, gives 1,350-fold purification with yields of about 60%. The toxin was shown to be a single-chain polypeptide of 140 kDa, pI 6.02. It was completely inactivated by heating at 56 degrees C...

Journal: :Infection and immunity 1985
J M Zhang J L Cowell A C Steven P H Carter P P McGrath C R Manclark

Fimbriae were detached from Bordetella pertussis by mechanical shearing and purified by successive precipitations with ammonium sulfate, phosphate buffer (pH 6.0), and magnesium chloride. In each of these purification steps, the fimbriae aggregated into bundles as seen by electron microscopy. These aggregates could be disaggregated at pH 9.5. By electron microscopy, the purified fimbriae appear...

Journal: :Pathogens and disease 1991
T Tomoda H Ogura T Kurashige

To assess antibody and cellular immune responses, 156 healthy children were immunized at approximately 18 months of age with acellular diphtheria-tetanus-pertussis vaccine. Changes in antibody responses to filamentous hemagglutinin (FHA) and to pertussis toxin (PT) were similar in pattern, and antibody titers reached values equal to those from patients with convalescent-stage pertussis. The FHA...

2012
Violette Dirix Virginie Verscheure Françoise Vermeulen Iris De Schutter Tessa Goetghebuer Camille Locht Françoise Mascart

Infant CD4⁺ T-cell responses to bacterial infections or vaccines have been extensively studied, whereas studies on CD8⁺ T-cell responses focused mainly on viral and intracellular parasite infections. Here we investigated CD8⁺ T-cell responses upon Bordetella pertussis infection in infants, children, and adults and pertussis vaccination in infants. Filamentous hemagglutinin-specific IFN-γ secret...

Journal: :Infection and immunity 1997
K Berggård E Johnsson F R Mooi G Lindahl

C4BP (C4b-binding protein) is a high-molecular-weight plasma protein that inhibits the classical pathway of complement activation. Recent experiments have demonstrated that C4BP binds to many strains of the gram-positive bacterium Streptococcus pyogenes, a major respiratory tract pathogen. Binding to S. pyogenes was shown to be due to members of the M protein family, a group of surface proteins...

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