Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter

Yeo, Hye‐Jeong; Cotter, Shane E.; Laarmann, Sven; Juehne, Twyla; Geme, Joseph W. St.; Waksman, Gabriel

doi:10.1038/sj.emboj.7600142

Cited by 90 publications

(108 citation statements)

References 32 publications

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“…2) (263). Recent structural investigations have demonstrated that the H. influenzae Hia adhesin is a trimeric protein secreted in a manner analogous to YadA rather than the true autotransporters, as previously described (465,474,541). This type of trimeric conformation and mode of secretion has been proposed as an alternative model for autotransporter secretion system (see above) and has been designated the type Vc or AT-2 pathway (Fig.…”

Section: Type Vcmentioning

confidence: 99%

Type V Protein Secretion Pathway: the Autotransporter Story

Henderson

Navarro-Garcı́a

Desvaux

et al. 2004

Microbiol Mol Biol Rev

713

795

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Gram-negative bacteria possess an outer membrane layer which constrains uptake and secretion of solutes and polypeptides. To overcome this barrier, bacteria have developed several systems for protein secretion. The type V secretion pathway encompasses the autotransporter proteins, the two-partner secretion system, and the recently described type Vc or AT-2 family of proteins. Since its discovery in the late 1980s, this family of secreted proteins has expanded continuously, due largely to the advent of the genomic age, to become the largest group of secreted proteins in gram-negative bacteria. Several of these proteins play essential roles in the pathogenesis of bacterial infections and have been characterized in detail, demonstrating a diverse array of function including the ability to condense host cell actin and to modulate apoptosis. However, most of the autotransporter proteins remain to be characterized. In light of new discoveries and controversies in this research field, this review considers the autotransporter secretion process in the context of the more general field of bacterial protein translocation and exoprotein function

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Section: Type Vcmentioning

confidence: 99%

Type V Protein Secretion Pathway: the Autotransporter Story

Henderson

Navarro-Garcı́a

Desvaux

et al. 2004

Microbiol Mol Biol Rev

713

795

View full text Add to dashboard Cite

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“…This fragment was digested with EcoRI and BamHI and then ligated to EcoRI/ BamHI-digested pGEX-6P-1 (GE Healthcare, Piscataway, NJ), generating pGEX::Cha70-473, which was transformed into E. coli DH5␣. Cultures of DH5␣/pGEX::Cha70-473 were incubated at 37°C to an optical density of 0.4 to 0.5, and then expression of the glutathione S-transferase (GST)-Cha fusion protein was induced with 0.1 mM isopropyl-␤-D thiogalactopyranoside at 30°C for 4 h. Purification of the GST-Cha protein was performed as described previously, with minor modifications (53). Briefly, cells were harvested and lysed by sonication in lysis buffer (5 mM EDTA and 1 mM Pefabloc SC [Roche] in phosphate-buffered saline, pH 7.4), and the protein was isolated from clarified supernatant by affinity chromatography with glutathione-Sepharose beads (Pierce) according to the manufacturer's instructions.…”

Section: Methodsmentioning

confidence: 99%

Identification of a Novel Trimeric Autotransporter Adhesin in the Cryptic Genospecies of Haemophilus

Sheets¹,

Grass²,

Miller

et al. 2008

J Bacteriol

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“…Hia is an autotransporter that mediates adherence to cultured epithelial cells via two distinct binding domains contained within residues 50-252 and 580-714, and it has a translocator domain contained within residues 1,023-1,098 (40)(41)(42)(43). Whole-cell sonicates and trichloroacetic acid-precipitated supernatant proteins generated from DH5␣ expressing either Hia or the HMW1-Hia chimeric protein in the presence of HMW1B were examined by immunoblot analysis.…”

Section: Hmw1b Interacts With the N-terminal Fragment Of Hmw1mentioning

confidence: 99%

Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution

Surana

Grass

Hardy

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Omp85-like proteins represent a family of proteins involved in protein translocation, and they are present in all domains of life, except archaea. In eukaryotes, Omp85-like proteins have been demonstrated to form tetrameric pore-forming complexes that interact directly with their substrate proteins. Studies performed with bacterial Omp85-like proteins have demonstrated pore-forming activity but no evidence of multimerization. In this article, we characterize the Haemophilus influenzae HMW1B protein, an Omp85-like protein that has been demonstrated to be critical for secretion of the H. influenzae HMW1 adhesin. Analysis of purified protein by biochemical and electron microscopic techniques revealed that HMW1B forms a tetramer. Examination using liposomeswelling assays demonstrated that HMW1B has pore-forming activity, with a pore size of Ϸ2.7 nm. Far-Western blot analysis established that HMW1B interacts with the N terminus of HMW1. These results provide evidence that a bacterial Omp85-like protein forms a tetramer and interacts directly with a substrate protein, suggesting that the architecture and physical properties of Omp85-like proteins have been conserved throughout evolution. O mp85-like proteins represent a large family defined by phylogenetic relatedness, secondary-structure predictions, and a role in protein translocation (1-5). Members of this family are present in diverse organisms across the evolutionary spectrum, including bacteria, fungi, plants, and animals (1, 4). The widespread nature of Omp85-like proteins underscores their critical role in cellular processes, highlighted by the fact that many are required for cell viability (3,4,(6)(7)(8)(9). Although all Omp85-like proteins share sequence homology, they can be grouped into two classes based on the specific role that they play in protein translocation. One class is typified by Saccharomyces cerevisiae Sam50 and Neurospora crassa Tob55, which are chiefly involved in insertion of ␤-barrel proteins into the outer membrane (OM) of mitochondria (6, 9). The second class is epitomized by the chloroplast protein Toc75, which is involved in secretion of proteins across a membrane (10, 11). Interestingly, both classes of Omp85-like proteins are present in Gramnegative bacteria. Neisseria meningitidis Omp85, the namesake of this family of proteins, has been demonstrated recently to be critical for the insertion of proteins into the bacterial OM (7). Other Gram-negative bacterial Omp85-like proteins, including Serratia marcescens ShlB and Bordetella pertussis FhaC [and other members of the so-called two-partner secretion (TPS) pathway], have been demonstrated to function in protein export across the OM (12).The high level of amino acid homology among Omp85-like proteins from bacteria to humans raises the possibility that members of this family have similar structures. Although no crystal structures exist so far for Omp85-like proteins, several of these proteins have been subjected to biochemical studies of overall architecture. In eukaryotes, both classes...

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Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter

Cited by 90 publications

References 32 publications

Type V Protein Secretion Pathway: the Autotransporter Story

Type V Protein Secretion Pathway: the Autotransporter Story

Identification of a Novel Trimeric Autotransporter Adhesin in the Cryptic Genospecies of Haemophilus

Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution

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