scholarly journals Helicobacter pyloriHopQ outer membrane protein attenuates bacterial adherence to gastric epithelial cells

2008 ◽  
Vol 289 (1) ◽  
pp. 53-58 ◽  
Author(s):  
John T. Loh ◽  
Victor J. Torres ◽  
Holly M. Scott Algood ◽  
Mark S. McClain ◽  
Timothy L. Cover
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Bacterial Adherence ◽  
Gastric Epithelial Cells

scholarly journals Identification of Functional Interactome of Gastric Cancer Cells with Helicobacter pylori Outer Membrane Protein HpaA by HPLC-MS/MS

2020 ◽  
Vol 2020 ◽  
pp. 1-10
Author(s):  
Ruyue Fan ◽  
Xiurui Han ◽  
Di Xiao ◽  
Lihua He ◽  
Yanan Gong ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Helicobacter Pylori ◽  
Epithelial Cells ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Cell Lines ◽  
Outer Membrane Protein ◽  
Regulation Of Transcription ◽  
Gastric Epithelial Cells ◽  
H Pylori

HpaA as an outer membrane protein of Helicobacter pylori (H. pylori) plays a significant role in the adhesion to the human stomach, but the functional relation between HpaA and gastric epithelial cells is still not clear. To screen the interaction between HpaA and cellular proteins in gastric epithelial cells, the HpaA protein from H. pylori 26695 fused with a tag (6× His) was expressed and purified successfully, the secondary structure was estimated by the Circular Dichroism (CD) spectrum, and the purified recombinant protein was used to perform the pull-down assays with gastric cancer cell lines (AGS and SGC-7901) lysates, respectively. The pull-down proteins were identified by high-performance liquid chromatography tandem mass spectrometry system (HPLC-MS/MS). A total of 9 and 13 proteins related were analyzed from AGS and SGC-7901 cell lysates, respectively. ANXA2 was considered as putative HpaA functional partner discovered from lysates of both cell lines with high score and coverage. It is hypothesized that HpaA may be involved in the biological process of regulation of transcription and nucleic acid metabolism during the adhesion of H. pylori to human gastric epithelial cells, and HpaA-binding proteins also be used as targets for the development of antiadhesion drugs against H. pylori.

scholarly journals The Immunoglobulin D-Binding Protein MID from Moraxella catarrhalis Is Also an Adhesin

2003 ◽  
Vol 71 (6) ◽  
pp. 3302-3309 ◽  
Author(s):  
Arne Forsgren ◽  
Marta Brant ◽  
Mirela Karamehmedovic ◽  
Kristian Riesbeck
Keyword(s):  
Amino Acid ◽  
Epithelial Cells ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Moraxella Catarrhalis ◽  
Binding Protein ◽  
Alveolar Epithelial Cells ◽  
Alveolar Epithelial ◽  
Immunoglobulin D

ABSTRACT The Moraxella catarrhalis immunoglobulin D (IgD)-binding protein (MID) is a 200-kDa outer membrane protein displaying a unique and specific affinity for human IgD. MID is found in the majority of M. catarrhalis strains. In the present paper, we show that MID-expressing M. catarrhalis strains agglutinate human erythrocytes and bind to type II alveolar epithelial cells. In contrast, M. catarrhalis isolates with low MID expression levels and two mutants deficient in MID, but with readily detectable UspA1 expression, do not agglutinate erythrocytes and have a 50% lower adhesive capacity. To examine the adhesive part of MID, the protein was dissected into nine fragments covering the entire molecule. The truncated MID proteins were expressed in Escherichia coli, purified, and used for raising polyclonal antibodies in rabbits. Interestingly, by using recombinant fragments, we show that the hemagglutinating and adhesive part of MID is localized within the 150-amino-acid fragment MID764-913. In addition, antibodies against full-length MID, MID764-913, or a 30-amino-acid consensus sequence (MID775-804) inhibited adhesion to alveolar epithelial cells. Antibodies against UspA1, an outer membrane protein expressed in essentially all M. catarrhalis strains, also inhibited adhesion, suggesting that both MID and UspA1 are needed for optimal attachment to epithelial cells. Taken together, in addition to MID-dependent IgD binding, we have demonstrated that the outer membrane protein MID is a novel adhesin that would be a suitable target for a future vaccine against M. catarrhalis.

Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells

2005 ◽  
Vol 7 (8) ◽  
pp. 1127-1138 ◽  
Author(s):  
Chul Hee Choi ◽  
Eun Young Lee ◽  
Yoo Chul Lee ◽  
Tae In Park ◽  
Hwa Jung Kim ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Acinetobacter Baumannii ◽  
Outer Membrane ◽  
Outer Membrane Protein

scholarly journals Bacterial entry and intracellular processing of Neisseria gonorrhoeae in epithelial cells: immunomorphological evidence for alterations in the major outer membrane protein P.IB.

1991 ◽  
Vol 174 (3) ◽  
pp. 705-715 ◽  
Author(s):  
J F Weel ◽  
C T Hopman ◽  
J P van Putten
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Host Cell ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Major Outer Membrane Protein ◽  
Host Cells ◽  
Eukaryotic Cells ◽  
Bacterial Invasion ◽  
Intracellular Processing

The fate of the major outer membrane protein of the gonococcus, P.IB, during the adherence, entry, and intracellular processing of the bacteria in infected epithelial cells was investigated using post-embedding immunoelectron microscopy. Various domains of the P.IB molecule were probed at different stages in the infection. These studies revealed that P.IB epitope exposure remained unaltered during the initial attachment of the bacteria to the host cells. In contrast, upon secondary attachment of the bacteria to the eukaryotic cells, apparent zones of adhesion were formed between the gonococci and the host cell membrane, which were characterized by loss of a defined P.IB epitope. These zones of adhesion with the altered P.IB immunoreactivity continued to exist and increased in number during cellular penetration, suggesting that they were essential to bacterial invasion into the eukaryotic cells. After bacterial entry, two classes of gonococci could be recognized; morphologically intact, P.IB-positive bacteria and disintegrated organisms that showed a change in, and, in a later stage, a complete loss of P.IB immunoreactivity. The intracellular alterations in the P.IB antigen could be prevented by treatment of the host cells with the lysosomotropic agent chloroquine. These observations point to a mechanism by which a subpopulation of intracellular gonococci can escape the epithelial cell defense by preventing or resisting exposure to host cell proteolytic activity.

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