A human endothelial cell membrane protein that binds Staphylococcus aureus in vitro.

Tompkins, David C.; Hatcher, Victor B.; Patel, Daxa; Orr, George A.; Higgins, Lore L.; Lowy, Franklin D.

doi:10.1172/jci114560

Cited by 51 publications

(52 citation statements)

References 32 publications

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“…Cytolysis of tumor cells by HPBL was measured as described previously (23,24 Staphylococcus aureus and human endothelial cell plasma membrane proteins (25). Initial studies were performed with the NK-sensitive K562 tumor cell line.…”

Section: Binding Of Tumor Plasma Membrane Proteins To Viable Lymfho-mentioning

confidence: 99%

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A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

Das

Mondragon

Sadeghian

et al. 1994

The Journal of Experimental Medicine

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126

109

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SummaryExtracellular adenosine triphosphate (eATP) has been suggested to play a role in lymphocyteinduced tumor destruction. We now provide evidence that a protein responsible for ATP synthesis in mitochondria may also play a physiologic role in major histocompatibility complex-independent, lymphocyte-mediated cytotoxicity. A 51.5-kD protein (p51.5) beating structural and immunologic characteristics of the B subunit of H + transporting ATP synthase (E.C. 3.6.1.34, B-H +ATPase, published molecular mass of 51.6 kD) was detected on the plasma membrane of three different human tumor cell lines studied. NH2-terminal amino acid sequence analysis of purified p51.5 from K562 tumor cells revealed 100% homology of 16 residues identified in the first 21 positions to the known sequence of human mitochondrial B-H § ATPase. Antibody directed against a 2l-iner peptide in the ATP binding region of B-H+ATPase (anti-B) reacted with only one band on Western blots of whole tumor extracts and tumor membrane extracts suggesting that the antiserum reacts with a single species of protein. Anti-B reacted with the cell membranes of tumor ceils as determined by fluorescence-activated flow cytometry and immunoprecipitated a 51.5-kD protein from surface-labeled neoplastic cells (but not human erythrocytes and lymphocytes). Purified p51.5 bound to human lymphocytes and inhibited natural killer (NK) cell-mediated cytotoxicity. Furthermore, anti-B treatment of the K562 and A549 tumor cell lines inhibited NK (by >95%) and interleukin 2-activated killer (LAK) cell (by 75%) cytotoxicity, respectively. Soluble p51.5 upon binding to lymphocytes retained its reactivity to anti-B suggesting that the ATP binding domain and the lymphocyte-receptor binding domain reside in distinct regions of the ligand. These results suggest that B-H +ATPase or a nearly identical molecule is an important ligand in the effector phase (rather than the recognition phase) of a cytolytic pathway used by naive NK and LAK cells.

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Section: Binding Of Tumor Plasma Membrane Proteins To Viable Lymfho-mentioning

confidence: 99%

“…and used to prepare plasma membranes as described previously (25). Plasma membrane proteins were solubilized with 1% Triton X-100 overnight at 4~ in a buffer containing 10 mM sodium borate, 10 mM benzamidine, 1 mM EDTA, 1 mM iodoacetamide, and I mM PMSF, pH 8.0 (buffer A).…”

mentioning

confidence: 99%

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

Das

Mondragon

Sadeghian

et al. 1994

The Journal of Experimental Medicine

Self Cite

126

109

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show abstract

“…Scavenger receptor class A (SR-A) 2 can bind Gram-positive (4) and Gram-negative (5) bacteria, including S. aureus and Escherichia coli, as well as lipoteichoic acid from Gram-positive bacteria (4) and LPS from Gramnegative bacteria (6). Studies with SR-A knockout mice revealed that SR-A plays important roles in host defense against bacterial infection; it enhances sensitivities for S. aureus (7) and Listeria infection (8) as well as for LPS-mediated septic shock (9).…”

mentioning

confidence: 99%

LOX-1 Supports Adhesion of Gram-Positive and Gram-Negative Bacteria

Shimaoka

Kume

Minami

et al. 2001

The Journal of Immunology

162

108

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Adhesion of bacteria to vascular endothelial cells as well as mucosal cells and epithelial cells appears to be one of the initial steps in the process of bacterial infection, including infective endocarditis. We examined whether lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1), a member of scavenger receptor family molecules with C-type lectin-like structure, can support adhesion of Gram-positive and Gram-negative bacteria. Chinese hamster ovary-K1 (CHO-K1) cells stably expressing LOX-1 can support binding of FITC-labeled Staphylococcus aureus and Escherichia coli, which was suppressed by poly(I) and an anti-LOX-1 mAb. Adhesion of these bacteria to LOX-1 does not require divalent cations or serum factors and can be supported under both static and nonstatic conditions. Cultured bovine aortic endothelial cells (BAEC) can also support adhesion of FITC-labeled S. aureus, which was similarly suppressed by poly(I) and an anti-LOX-1 mAb. In contrast, binding of FITC-labeled E. coli to BAEC was partially inhibited by the anti-LOX-1 mAb, and poly(I) did not block FITC-labeled E. coli adhesion to BAEC, but, rather, enhanced it under a static condition. TNF-α increased LOX-1-dependent adhesion of E. coli, but not that of S. aureus, suggesting that S. aureus adhesion to BAEC may require additional molecules, which cooperate with LOX-1 and suppressed by TNF-α. Taken together, LOX-1 can work as a cell surface receptor for Gram-positive and Gram-negative bacteria, such as S. aureus and E. coli, in a mechanism similar to that of class A scavenger receptors; however, other unknown molecules may also be involved in the adhesion of E. coli to BAEC, which is enhanced by poly(I).

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“…Salah satu contoh adalah Fim H vaccine yang sedang dikembangkan untuk mencegah infeksi saluran kemih yang disebabkan E. coli [5]. Kemampuan bakteri untuk melekat dan menembus sel endotel merupakan akibat dari interaksi adhesin-reseptor antara bakteri dan permukaan sel endotel [6]. Molekul reseptor tergantung pada jenis bakteri.…”

Section: Abstrakunclassified

Identifikasi Molekul Adhesi Pili Pseudomonas aeruginosa pada Human Umbilical Vein Endothelial Cells (HUVECs) Culture

Hidayati

2010

JELS

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AbstrakPseudomonas aeruginosa merupakan salah satu penyebab Gram negatif bakteriemia yang bisa berlanjut menjadi sepsis. Bakteri ini banyak menginfeksi penderita di rumah sakit dengan membentuk koloni pada pembuluh darah melalui proses adhesi (pelekatan). Pili dan bagian Outer Membrane Protein (OMP) adalah faktor yang mempengaruhi pelekatan bakteri P. aeruginosa. Tujuan dari penelitian ini adalah untuk mengetahui berat molekul protein hemaglutinin yang terdapat pada pili dan membuktikan peran protein hemaglutinin pada pili dalam pelekatan bakteri P. aeruginosa. Metode yang digunakan dalam penelitian ini adalah isolasi protein pili P. aeruginosa secara bertingkat, dilanjutkan dengan uji hemaglutinasi (metode mikrotiter) dan uji adhesi menggunakan protein pili hasil elektroelusi yang disalutkan pada kultur sel endotel (HUVECs) (konsentrasi 1, ½, ¼, ⅛, ⅟16 dan 0 [kontrol]). Hasil penelitian menunjukkan adanya reaksi hemaglutinasi pada potongan pili ketiga dengan titer tertinggi (1/128). Protein hemaglutinin dengan berat molekul 38,19 kDa memberikan titer tertinggi (⅟16). Hasil uji adhesi protein hemaglutinin yang disalutkan pada sel endotel menunjukkan bahwa semakin tinggi pengenceran maka adhesi bakteri menunjukkan peningkatan secara signifikan dengan konstanta regresi (r)= 0,98 dan p value= 0,00. Berdasarkan penelitian dapat disimpulkan bahwa protein hemaglutinin pili merupakan protein adhesin. Protein adhesin dengan berat molekul 38,19 kDa berperan pada perlekatan bakteri P. aeruginosa 9064 dengan kultur sel endotel (HUVECs). Kontak langsung antara agen infeksi dengan sel inang diawali dengan proses adhesi (perlekatan) [3]. Bakteri P. aeruginosa dapat melakukan adhesi dan membentuk koloni pada bermacam-macam tipe sel yaitu epitel sel buccal, paru, ginjal dan sel endothel [3]. Adhesin bakteri Gram negatif diperankan oleh suatu protein yang mampu mengaglutinasi eritrosit mamalia protein ini disebut dengan protein hemaglutinin, salah satu contoh adalah protein adhesin Klebsiella pneumoniae yang diperankan oleh protein hemaglutinin 29 kDa [4].Penemuan bahwa adhesi merupakan tahap awal proses infeksi pada sebagian besar bakteri, menunjukkan bahwa protein adhesin tersebut memiliki potensi sebagai komponen vaksin yang baik. Salah satu contoh adalah Fim H vaccine yang sedang dikembangkan untuk mencegah infeksi saluran kemih yang disebabkan E. coli [5]. Kemampuan bakteri untuk melekat dan menembus sel endotel merupakan akibat dari interaksi adhesin-reseptor antara bakteri dan permukaan sel endotel [6]. Molekul reseptor tergantung pada jenis bakteri. Molekul reseptor terdapat di enterosit epitel vesica urinaria atau endotel. Bakteri Pseudomonas aeruginosa melekat selektif terhadap sel-sel endotel manusia [7].

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A human endothelial cell membrane protein that binds Staphylococcus aureus in vitro.

Cited by 51 publications

References 32 publications

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

LOX-1 Supports Adhesion of Gram-Positive and Gram-Negative Bacteria

Identifikasi Molekul Adhesi Pili Pseudomonas aeruginosa pada Human Umbilical Vein Endothelial Cells (HUVECs) Culture

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