Distinct roles of the N-terminal and C-terminal precursor domains in the biogenesis of the Bordetella pertussis filamentous hemagglutinin.
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Bordetella filamentous hemagglutinin plays a critical role in immunomodulation, suggesting a mechanism for host specificityRole of adhesin release for mucosal colonization by a bacterial pathogenThe structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretionSubtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway.Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.The prodomain of the Bordetella two-partner secretion pathway protein FhaB remains intracellular yet affects the conformation of the mature C-terminal domain.Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membraneType V Secretion: the Autotransporter and Two-Partner Secretion PathwaysCharacterization of a novel two-partner secretion system in Escherichia coli O157:H7.Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin.Mechanism of association of adenylate cyclase toxin with the surface of Bordetella pertussis: a role for toxin-filamentous haemagglutinin interaction.Antigenic analysis of Bordetella pertussis filamentous hemagglutinin with phage display libraries and rabbit anti-filamentous hemagglutinin polyclonal antibodiesType V protein secretion pathway: the autotransporter storyTwo-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria InteractionsHaemophilus ducreyi secretes a filamentous hemagglutinin-like protein.Filamentous hemagglutinin of Bordetella bronchiseptica is required for efficient establishment of tracheal colonizationCharacterization of the filamentous hemagglutinin-like protein FhaS in Bordetella bronchisepticaProduction of Neisseria meningitidis transferrin-binding protein B by recombinant Bordetella pertussisImmunogenicity of live attenuated B. pertussis BPZE1 producing the universal influenza vaccine candidate M2e.Sequential translocation of an Escherchia coli two-partner secretion pathway exoprotein across the inner and outer membranesAntibodies specific for the high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are opsonophagocytic for both homologous and heterologous strains.Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineriesAutotransporter and two-partner secretion: delivery of large-size virulence factors by gram-negative bacterial pathogens.Natural-host animal models indicate functional interchangeability between the filamentous haemagglutinins of Bordetella pertussis and Bordetella bronchiseptica and reveal a role for the mature C-terminal domain, but not the RGD motif, during infectiContribution of Bordetella bronchiseptica filamentous hemagglutinin and pertactin to respiratory disease in swine.Induction of mucosal immune responses against a heterologous antigen fused to filamentous hemagglutinin after intranasal immunization with recombinant Bordetella pertussis.The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway.Pertussis: a matter of immune modulation.Filamentous hemagglutinin of Bordetella pertussis: a key adhesin with immunomodulatory properties?Eighty-kilodalton N-terminal moiety of Bordetella pertussis filamentous hemagglutinin: adherence, immunogenicity, and protective role.VirB1, a component of the T-complex transfer machinery of Agrobacterium tumefaciens, is processed to a C-terminal secreted product, VirB1.Production of nontypeable Haemophilus influenzae HtrA by recombinant Bordetella pertussis with the use of filamentous hemagglutinin as a carrier.Characterization of serological responses to pertussis.System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin.
P2860
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P2860
Distinct roles of the N-terminal and C-terminal precursor domains in the biogenesis of the Bordetella pertussis filamentous hemagglutinin.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Distinct roles of the N-termin ...... sis filamentous hemagglutinin.
@en
Distinct roles of the N-termin ...... sis filamentous hemagglutinin.
@nl
type
label
Distinct roles of the N-termin ...... sis filamentous hemagglutinin.
@en
Distinct roles of the N-termin ...... sis filamentous hemagglutinin.
@nl
prefLabel
Distinct roles of the N-termin ...... sis filamentous hemagglutinin.
@en
Distinct roles of the N-termin ...... sis filamentous hemagglutinin.
@nl
P2093
P2860
P1476
Distinct roles of the N-termin ...... ssis filamentous hemagglutinin
@en
P2093
F D Menozzi
G Renauld-Mongénie
J Cornette
P2860
P304
P356
10.1128/JB.178.4.1053-1060.1996
P577
1996-02-01T00:00:00Z