scholarly journals Adhesion of Escherichia coli to HeLa Cells Mediated byTrypanosoma cruzi Surface Glycoprotein-Derived Peptides Inserted in the Outer Membrane Protein LamB

1999 ◽  
Vol 67 (9) ◽  
pp. 4908-4911 ◽  
Author(s):  
Cátia M. Pereira ◽  
Sílvio Favoreto ◽  
José Franco da Silveira ◽  
Nobuko Yoshida ◽  
Beatriz A. Castilho
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Cell Surface ◽  
Hela Cells ◽  
Outer Membrane Protein ◽  
Fusion Proteins ◽  
Mammalian Cells ◽  
Host Cells ◽  
Surface Glycoprotein ◽  
Parasite Invasion

ABSTRACT Peptides derived from the surface glycoprotein gp82 ofTrypanosoma cruzi, previously implicated in the parasite’s invasion of host cells, were expressed as fusions to the protein LamB of Escherichia coli in a region known to be exposed on the cell surface. Bacteria expressing these proteins adhered to HeLa cells in a manner that mimics the pattern of parasite invasion of mammalian cells. Purified LamB fusion proteins were shown to bind to HeLa cells and to inhibit infection by T. cruzi, supporting the notion that these gp82-derived peptides can mediate interaction of the parasite with its host.

Assessing Changes in the Expression Levels of Cell Surface Proteins with a Turn-on Fluorescent Molecular Probe

2021 ◽  
Author(s):  
Joydev Hatai ◽  
Pragati Kishore Prasad ◽  
Naama Mankovski ◽  
Noa Oppenheimer ◽  
Tamar Unger ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Cell Surface ◽  
Outer Membrane Protein ◽  
Protein C ◽  
Nitrilotriacetic Acid ◽  
Surface Proteins ◽  
Molecular Probe ◽  
Cell Surface Proteins ◽  
Turn On

Tri-nitrilotriacetic acid (NTA)-based fluorescent probes were developed and used to image His-tagged-labelled outer membrane protein C (His-OmpC) in live Escherichia coli. One of these probes was designed to light up...

scholarly journals β1-Chain Integrins Are Not Essential for Intimin-Mediated Host Cell Attachment and EnteropathogenicEscherichia coli-Induced Actin Condensation

1999 ◽  
Vol 67 (4) ◽  
pp. 2045-2049 ◽  
Author(s):  
Hui Liu ◽  
Loranne Magoun ◽  
John M. Leong
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Outer Membrane Protein ◽  
Mammalian Cells ◽  
Actin Polymerization ◽  
Cell Attachment ◽  
Gene Encoding ◽  
Host Cell Attachment ◽  
Integrin Antagonists ◽  
Bacterial Outer Membrane

ABSTRACT Intimin is a bacterial outer membrane protein required for intimate attachment of enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) to mammalian cells. β1-chain integrins have been proposed as candidate receptors for intimin. We found that binding of mammalian cells to immobilized intimin was not detectable unless mammalian cells were preinfected with EPEC or EHEC. β1-chain integrin antagonists or inactivation of the gene encoding the β1-chain did not affect binding of preinfected mammalian cells to intimin or the actin condensation associated with the attachment of EPEC. The results indicate that β1-chain integrins are not essential for intimin-mediated cell attachment or EPEC-mediated actin polymerization.

scholarly journals Mechanical Fractionation Reveals Structural Requirements for Enteropathogenic Escherichia coli Tir Insertion into Host Membranes

2000 ◽  
Vol 68 (7) ◽  
pp. 4344-4348 ◽  
Author(s):  
Annick Gauthier ◽  
Myriam de Grado ◽  
B. Brett Finlay
Keyword(s):  
Escherichia Coli ◽  
Host Cell ◽  
Hela Cells ◽  
Protein Delivery ◽  
Mammalian Cells ◽  
Host Cells ◽  
Host Cell Membrane ◽  
Bacterial Proteins ◽  
Host Cell Membranes ◽  
Triton X

ABSTRACT Enteropathogenic Escherichia coli (EPEC) inserts its receptor for intimate adherence (Tir) into host cell membranes by using a type III secretion system. Detergents are frequently used to fractionate infected host cells to investigate bacterial protein delivery into mammalian cells. In this study, we found that the Triton X-100-soluble membrane fraction from EPEC-infected HeLa cells was contaminated with bacterial proteins. We therefore applied a mechanical method of cell lysis and ultracentrifugation to fractionate infected HeLa cells to investigate the biology and biochemistry of Tir delivery and translocation. This method demonstrates that the translocation of Tir into the host cell membrane requires its transmembrane domains, but not tyrosine phosphorylation or binding to Tir's ligand, intimin.

Role of the cell surface-exposed regions of outer membrane protein PhoE of Escherichia coli K12 in the biogenesis of the protein

1989 ◽  
Vol 185 (2) ◽  
pp. 365-370 ◽  
Author(s):  
Marja AGTERBERG ◽  
Henriette ADRIAANSE ◽  
Edwin TIJHAAR ◽  
Annelies RESINK ◽  
Jan TOMMASSEN
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Cell Surface ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Escherichia Coli K12

Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12

1986 ◽  
Vol 188 (3) ◽  
pp. 491-494 ◽  
Author(s):  
Roland Freudl ◽  
Sheila MacIntyre ◽  
Maria Degen ◽  
Ulf Henning
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Cell Surface ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
K 12

Overexpression of Outer Membrane Protein A Is a Risk Factor for Mortality in Escherichia coli Bloodstream Infections

2019 ◽  
Author(s):  
Ángel Rodríguez-Villodres ◽  
Rocío Álvarez-Marín ◽  
María Antonia Pérez-Moreno ◽  
Andrea Miró-Canturri ◽  
Marco Durán Lobato ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Risk Factor ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Bloodstream Infections ◽  
Outer Membrane Protein A

scholarly journals A Single-Pass Type I Membrane Protein from the Apicomplexan Parasite Cryptosporidium parvum with Nanomolar Binding Affinity to Host Cell Surface

2021 ◽  
Vol 9 (5) ◽  
pp. 1015
Author(s):  
Tianyu Zhang ◽  
Xin Gao ◽  
Dongqiang Wang ◽  
Jixue Zhao ◽  
Nan Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Host Cell ◽  
Binding Affinity ◽  
Cryptosporidium Parvum ◽  
Host Cells ◽  
Watery Diarrhea ◽  
Type I ◽  
Single Pass ◽  
Host Cell Surface

Cryptosporidium parvum is a globally recognized zoonotic parasite of medical and veterinary importance. This parasite mainly infects intestinal epithelial cells and causes mild to severe watery diarrhea that could be deadly in patients with weakened or defect immunity. However, its molecular interactions with hosts and pathogenesis, an important part in adaptation of parasitic lifestyle, remain poorly understood. Here we report the identification and characterization of a C. parvum T-cell immunomodulatory protein homolog (CpTIPH). CpTIPH is a 901-aa single-pass type I membrane protein encoded by cgd5_830 gene that also contains a short Vibrio, Colwellia, Bradyrhizobium and Shewanella (VCBS) repeat and relatively long integrin alpha (ITGA) N-terminus domain. Immunofluorescence assay confirmed the location of CpTIPH on the cell surface of C. parvum sporozoites. In congruence with the presence of VCBS repeat and ITGA domain, CpTIPH displayed high, nanomolar binding affinity to host cell surface (i.e., Kd(App) at 16.2 to 44.7 nM on fixed HCT-8 and CHO-K1 cells, respectively). The involvement of CpTIPH in the parasite invasion is partly supported by experiments showing that an anti-CpTIPH antibody could partially block the invasion of C. parvum sporozoites into host cells. These observations provide a strong basis for further investigation of the roles of CpTIPH in parasite-host cell interactions.

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