-
1
-
-
0017168730
-
Resistance of Neisseria gonorrhoeae grown in vivo to ingestion and digestion by phagocytes of human blood
-
Witt K, Veale DR, Finch H, Penn CW, Sen D, Smith H Resistance of Neisseria gonorrhoeae grown in vivo to ingestion and digestion by phagocytes of human blood. J Gen Microbiol. 96:1976;341-350.
-
(1976)
J Gen Microbiol
, vol.96
, pp. 341-350
-
-
Witt, K.1
Veale, D.R.2
Finch, H.3
Penn, C.W.4
Sen, D.5
Smith, H.6
-
2
-
-
0019522910
-
Pathogenic mechanisms of Neisseria gonorrhoeae: Observations on damage to human fallopian tubes in organ culture by gonococci of colony type 1 or type 4
-
McGee ZA, Johnson AP, Taylor-Robinson D Pathogenic mechanisms of Neisseria gonorrhoeae: observations on damage to human fallopian tubes in organ culture by gonococci of colony type 1 or type 4. J Infect Dis. 143:1981;413-422.
-
(1981)
J Infect Dis
, vol.143
, pp. 413-422
-
-
McGee, Z.A.1
Johnson, A.P.2
Taylor-Robinson, D.3
-
3
-
-
0029116378
-
Interaction of pathogenic Neisseriae with nonphagocytic cells
-
Nassif X, So M Interaction of pathogenic Neisseriae with nonphagocytic cells. Clin Microbiol Rev. 8:1995;376-388.
-
(1995)
Clin Microbiol Rev
, vol.8
, pp. 376-388
-
-
Nassif, X.1
So, M.2
-
4
-
-
0028829320
-
Structure of the fibre-forming protein pilin at 2.6 Å resolution
-
Parge HE, Forest KT, Hickey MJ, Christensen DA, Getzoff ED, Tainer JA Structure of the fibre-forming protein pilin at 2.6 Å resolution. Nature. 378:1995;32-38.
-
(1995)
Nature
, vol.378
, pp. 32-38
-
-
Parge, H.E.1
Forest, K.T.2
Hickey, M.J.3
Christensen, D.A.4
Getzoff, E.D.5
Tainer, J.A.6
-
5
-
-
0026021682
-
Phase variation of gonococcal pili by frameshift mutation in pilC, a novel gene for pilus assembly
-
Jonsson AB, Nyberg G, Normark S Phase variation of gonococcal pili by frameshift mutation in pilC, a novel gene for pilus assembly. EMBO J. 10:1991;477-488.
-
(1991)
EMBO J
, vol.10
, pp. 477-488
-
-
Jonsson, A.B.1
Nyberg, G.2
Normark, S.3
-
6
-
-
0028795092
-
Neisseria PilC protein identified as type-4 pilus tip-located adhesin
-
Rudel T, Scheurerpflug I, Meyer TF Neisseria PilC protein identified as type-4 pilus tip-located adhesin. Nature. 373:1995;357-359.
-
(1995)
Nature
, vol.373
, pp. 357-359
-
-
Rudel, T.1
Scheurerpflug, I.2
Meyer, T.F.3
-
7
-
-
0031017899
-
PilC of Neisseria meningitidis is involved in class II pilus formation and restores pilus assembly, natural transformation competence and adherence to epithelial cells in PilC-deficient gonococci
-
Ryll RR, Rudel T, Scheuerpflug I, Barten R, Meyer TF PilC of Neisseria meningitidis is involved in class II pilus formation and restores pilus assembly, natural transformation competence and adherence to epithelial cells in PilC-deficient gonococci. Mol Microbiol. 23:1997;879-892.
-
(1997)
Mol Microbiol
, vol.23
, pp. 879-892
-
-
Ryll, R.R.1
Rudel, T.2
Scheuerpflug, I.3
Barten, R.4
Meyer, T.F.5
-
8
-
-
0026446170
-
Interaction of two variable proteins (PilE and PilC) required for pilus-mediated adherence of Neisseria gonorrhoeae to human epithelial cells
-
Rudel T, Van Putten JPM, Gibbs CP, Haas R, Meyer TF Interaction of two variable proteins (PilE and PilC) required for pilus-mediated adherence of Neisseria gonorrhoeae to human epithelial cells. Mol Microbiol. 6:1992;3439-3450.
-
(1992)
Mol Microbiol
, vol.6
, pp. 3439-3450
-
-
Rudel, T.1
Van Putten, J.P.M.2
Gibbs, C.P.3
Haas, R.4
Meyer, T.F.5
-
9
-
-
85087235588
-
Roles of PilC and PilE proteins in pilus-mediated adherence of Neisseria gonorrhoeae and Neisseria meningitidis to human erythrocytes, endothelial and epithelial cells
-
in press
-
Scheuerpflug I, Rudel T, Ryll R, Pandit J, Meyer TF: Roles of PilC and PilE proteins in pilus-mediated adherence of Neisseria gonorrhoeae and Neisseria meningitidis to human erythrocytes, endothelial and epithelial cells. Infect Immun 1998, in press.
-
(1998)
Infect Immun
-
-
Scheuerpflug, I.1
Rudel, T.2
Ryll, R.3
Pandit, J.4
Meyer, T.F.5
-
10
-
-
0030779080
-
Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
-
Kallstrom H, Liszewski MK, Atkinson JP, Jonsson AB Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria. Mol Microbiol. 25:1997;639-647.
-
(1997)
Mol Microbiol
, vol.25
, pp. 639-647
-
-
Kallstrom, H.1
Liszewski, M.K.2
Atkinson, J.P.3
Jonsson, A.B.4
-
11
-
-
0032555594
-
Cell signaling by the type IV pili of pathogenic Neisseria
-
2+ inhibited pilus adherence suggesting the up-regulation of pilus receptors by CD46 mediated pathways
-
2+ inhibited pilus adherence suggesting the up-regulation of pilus receptors by CD46 mediated pathways.
-
(1998)
J Biol Chem
, vol.273
, pp. 21777-21782
-
-
Kallstrom, H.1
Islam, S.2
Berggren, P.O.3
Jonsson, A.B.4
-
12
-
-
0018186964
-
Studies on gonococcus infection. XV. Identification of surface proteins of Neisseria gonorrhoeae correlated with leukocyte association
-
King GJ, Swanson J Studies on gonococcus infection. XV. Identification of surface proteins of Neisseria gonorrhoeae correlated with leukocyte association. Infect Immun. 21:1978;575-584.
-
(1978)
Infect Immun
, vol.21
, pp. 575-584
-
-
King, G.J.1
Swanson, J.2
-
13
-
-
0019469737
-
Structural comparison of Neisseria gonorrhoeae outer membrane proteins
-
Heckels JE Structural comparison of Neisseria gonorrhoeae outer membrane proteins. J Bacteriol. 145:1981;736-742.
-
(1981)
J Bacteriol
, vol.145
, pp. 736-742
-
-
Heckels, J.E.1
-
14
-
-
0028958307
-
Gonococcal opacity: Lectin-like interactions between Opa proteins and lipooligosaccharide
-
Blake MS, Blake CM, Apicella MA, Mandrell RE Gonococcal opacity: lectin-like interactions between Opa proteins and lipooligosaccharide. Infect Immun. 63:1995;1434-1439.
-
(1995)
Infect Immun
, vol.63
, pp. 1434-1439
-
-
Blake, M.S.1
Blake, C.M.2
Apicella, M.A.3
Mandrell, R.E.4
-
15
-
-
0026453756
-
Genetic variation in pathogenic bacteria
-
Robertson BD, Meyer TF Genetic variation in pathogenic bacteria. Trends Gen. 8:1992;422-427.
-
(1992)
Trends Gen
, vol.8
, pp. 422-427
-
-
Robertson, B.D.1
Meyer, T.F.2
-
16
-
-
0025897153
-
Phase variation of the opacity outer membrane protein controls invasion by Neisseria gonorrhoeae into human epithelial cells
-
Makino S, van Putten JPM, Meyer TF Phase variation of the opacity outer membrane protein controls invasion by Neisseria gonorrhoeae into human epithelial cells. EMBO J. 10:1991;1307-1315.
-
(1991)
EMBO J
, vol.10
, pp. 1307-1315
-
-
Makino, S.1
Van Putten, J.P.M.2
Meyer, T.F.3
-
17
-
-
0027398024
-
Variable opacity (Opa) outer membrane proteins account for the cell tropisms displayed by Neisseria gonorrhoeae for human leukocytes and epithelial cells
-
Kupsch EM, Knepper B, Kuroki T, Heuer I, Meyer TF Variable opacity (Opa) outer membrane proteins account for the cell tropisms displayed by Neisseria gonorrhoeae for human leukocytes and epithelial cells. EMBO J. 12:1993;641-650.
-
(1993)
EMBO J
, vol.12
, pp. 641-650
-
-
Kupsch, E.M.1
Knepper, B.2
Kuroki, T.3
Heuer, I.4
Meyer, T.F.5
-
18
-
-
0029027169
-
Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells
-
van Putten JPM, Paul SM Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells. EMBO J. 14:1995;2144-2154.
-
(1995)
EMBO J
, vol.14
, pp. 2144-2154
-
-
Van Putten, J.P.M.1
Paul, S.M.2
-
20
-
-
0029905022
-
CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins
-
Chen T, Gotschlich EC CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins. Proc Natl Acad Sci USA. 93:1996;14851-14856.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 14851-14856
-
-
Chen, T.1
Gotschlich, E.C.2
-
21
-
-
0029848536
-
Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic Neisseriae
-
Virji M, Makepeace K, Ferguson DJ, Watt SM Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic Neisseriae. Mol Microbiol. 22:1996;941-950.
-
(1996)
Mol Microbiol
, vol.22
, pp. 941-950
-
-
Virji, M.1
Makepeace, K.2
Ferguson, D.J.3
Watt, S.M.4
-
22
-
-
0030965374
-
CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes
-
A thorough study describing the identification of CD66 as receptors for Opa proteins (see also previous reports [20,21]). The authors demonstrate that four different CD66 members synthesised in transfected HeLa cells mediate adherence and invasion by N. gonorrhoeae-expressing Opa
-
Gray-Owen SD, Dehio C, Haude A, Grunert F, Meyer TF CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes. EMBO J. 16:1997;3435-3445. A thorough study describing the identification of CD66 as receptors for Opa proteins (see also previous reports [20,21]). The authors demonstrate that four different CD66 members synthesised in transfected HeLa cells mediate adherence and invasion by N. gonorrhoeae-expressing Opa.
-
(1997)
EMBO J
, vol.16
, pp. 3435-3445
-
-
Gray-Owen, S.D.1
Dehio, C.2
Haude, A.3
Grunert, F.4
Meyer, T.F.5
-
23
-
-
0025729599
-
In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: Apparent role of Opa proteins in cellular invasion
-
Weel JF, Hopman CT, van Putten JPM In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: apparent role of Opa proteins in cellular invasion. J Exp Med. 173:1991;1395-1405.
-
(1991)
J Exp Med
, vol.173
, pp. 1395-1405
-
-
Weel, J.F.1
Hopman, C.T.2
Van Putten, J.P.M.3
-
24
-
-
0030660196
-
Syndecans: Multifunctional cell-surface co-receptors
-
Carey DJ Syndecans: multifunctional cell-surface co-receptors. Biochem J. 327:1997;1-16.
-
(1997)
Biochem J
, vol.327
, pp. 1-16
-
-
Carey, D.J.1
-
25
-
-
0031029922
-
Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells
-
50) into CHO cells. In addition, vitronectin was shown to bind to N. gonorrhoeaae producing OpaA rather than to other variant Opa proteins expressed in defined strains
-
50) into CHO cells. In addition, vitronectin was shown to bind to N. gonorrhoeaae producing OpaA rather than to other variant Opa proteins expressed in defined strains.
-
(1997)
Infect Immun
, vol.65
, pp. 964-970
-
-
Duensing, T.D.1
Van Putten, J.P.M.2
-
27
-
-
0032489349
-
v integrin receptors
-
v integrin-dependent uptake in vitronectin-stimulated epithelial cell invasion of N. gonorrhoeae
-
v integrin-dependent uptake in vitronectin-stimulated epithelial cell invasion of N. gonorrhoeae.
-
(1998)
FEBS Lett
, vol.424
, pp. 84-88
-
-
Dehio, M.1
Gomez-Duarte, O.G.2
Dehio, C.3
Meyer, T.F.4
-
28
-
-
0031871416
-
Entry of OpaA(+) gonococci into Hep-2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors
-
50) invasin-mediated entry of N. gonorrhoeae into HEp-2 cells via heparan sulfate proteoglycans (HSPG). Inhibition studies using heparanase, RGD-containing peptides and anti-α5 β1 integrin antibodies suggest fibronectin as a molecular bridge between HSPG and integrins, promoting invasion into HEp-2 cells
-
50) invasin-mediated entry of N. gonorrhoeae into HEp-2 cells via heparan sulfate proteoglycans (HSPG). Inhibition studies using heparanase, RGD-containing peptides and anti-α5 β1 integrin antibodies suggest fibronectin as a molecular bridge between HSPG and integrins, promoting invasion into HEp-2 cells.
-
(1998)
Mol Microbiol
, vol.29
, pp. 369-379
-
-
Van Putten, J.P.M.1
Duensing, T.2
Cole, R.L.3
-
29
-
-
0026048664
-
Carcinoembryonic antigen gene family: Molecular biology and clinical perspectives
-
Thompson JA, Grunert F, Zimmermann W Carcinoembryonic antigen gene family: molecular biology and clinical perspectives. J Clin Lab Anal. 5:1991;344-366.
-
(1991)
J Clin Lab Anal
, vol.5
, pp. 344-366
-
-
Thompson, J.A.1
Grunert, F.2
Zimmermann, W.3
-
31
-
-
0030709395
-
Differential Opa specificities for CD66 receptors influence tissue interactions and cellular response to Neisseria gonorrhoeae
-
The authors defined different specificity groups of Opa proteins interacting with CD66 receptors. The competence of individual Opas to interact with CD66a was strictly correlated with their ability to induce an oxidative response by polymorphonuclear granulocytes. Endothelial cells upregulate CD66 expression upon treatment with the proinflammatory cytokine tumour necrosis factor-α
-
Gray-Owen SD, Lorenzen DR, Haude A, Meyer TF, Dehio C Differential Opa specificities for CD66 receptors influence tissue interactions and cellular response to Neisseria gonorrhoeae. Mol Microbiol. 26:1997;971-980. The authors defined different specificity groups of Opa proteins interacting with CD66 receptors. The competence of individual Opas to interact with CD66a was strictly correlated with their ability to induce an oxidative response by polymorphonuclear granulocytes. Endothelial cells upregulate CD66 expression upon treatment with the proinflammatory cytokine tumour necrosis factor-α
-
(1997)
Mol Microbiol
, vol.26
, pp. 971-980
-
-
Gray-Owen, S.D.1
Lorenzen, D.R.2
Haude, A.3
Meyer, T.F.4
Dehio, C.5
-
32
-
-
0031011324
-
Differential recognition of members of the carcinoembryonic antigen family by Opa variants of Neisseria gonorrhoeae
-
•]. HeLa cells transfected with CD66 family members were used to functionally define their interactions with variant Opa proteins
-
•]. HeLa cells transfected with CD66 family members were used to functionally define their interactions with variant Opa proteins.
-
(1997)
Infect Immun
, vol.65
, pp. 2353-2361
-
-
Bos, M.P.1
Grunert, F.2
Belland, R.J.3
-
33
-
-
0031736077
-
Opa binding to cellular CD66 receptors mediates the trancellular traversal of Neisseria gonorrhoeae across polarized T84 epithelial cell monolayers
-
50, bind to CD66 receptors and exert transepithelial traversal. The transcytosis of N. gonorrhoeae does not detectably disrupt the barrier function of infected monolayers. Confocal laser and electronmicroscopy analysis suggest a transcellular rather than a paracellular route of traversal across the monolayer
-
50, bind to CD66 receptors and exert transepithelial traversal. The transcytosis of N. gonorrhoeae does not detectably disrupt the barrier function of infected monolayers. Confocal laser and electronmicroscopy analysis suggest a transcellular rather than a paracellular route of traversal across the monolayer.
-
(1998)
Mol Microbiol
, vol.30
, pp. 657-671
-
-
Wang, J.1
Gray-Owen, S.D.2
Knorre, A.3
Meyer, T.F.4
Dehio, C.5
-
34
-
-
0031983016
-
Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: Intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth
-
+ N. gonorrhoeae with PK in infected epithelial cells
-
+ N. gonorrhoeae with PK in infected epithelial cells.
-
(1998)
Mol Microbiol
, vol.27
, pp. 171-186
-
-
Williams, J.M.1
Chen, G.C.2
Zhu, L.3
Rest, R.F.4
-
35
-
-
0028284205
-
Variable expression of the Opc outer membrane protein in Neisseria meningitidis is caused by size variation of a promoter containing poly-cytidine
-
Sarkari J, Pandit N, Moxon ER, Achtman M Variable expression of the Opc outer membrane protein in Neisseria meningitidis is caused by size variation of a promoter containing poly-cytidine. Mol Microbiol. 13:1994;207-217.
-
(1994)
Mol Microbiol
, vol.13
, pp. 207-217
-
-
Sarkari, J.1
Pandit, N.2
Moxon, E.R.3
Achtman, M.4
-
36
-
-
0027524614
-
Meningococcal Opa and Opc proteins: Their role in colonization and invasion of human epithelial and endothelial cells
-
Virji M, Makepeace K, Ferguson DJ, Achtman M, Moxon ER Meningococcal Opa and Opc proteins: their role in colonization and invasion of human epithelial and endothelial cells. Mol Microbiol. 10:1993;499-510.
-
(1993)
Mol Microbiol
, vol.10
, pp. 499-510
-
-
Virji, M.1
Makepeace, K.2
Ferguson, D.J.3
Achtman, M.4
Moxon, E.R.5
-
37
-
-
0031884247
-
Neisseria meningitidis producing the Opc adhesin binds epithelial cell proteogylcan receptors
-
De Vries FP, Colgan SP, Dankert J, Frosch M, Van Putten JPM Neisseria meningitidis producing the Opc adhesin binds epithelial cell proteogylcan receptors. Mol Microbiol. 27:1998;1203-1212.
-
(1998)
Mol Microbiol
, vol.27
, pp. 1203-1212
-
-
De Vries, F.P.1
Colgan, S.P.2
Dankert, J.3
Frosch, M.4
Van Putten, J.P.M.5
-
38
-
-
0030930267
-
A proposed role for the lutropin receptor in contact-inducible gonococcal invasion of Hec1B cells
-
Unknown N. gonorrhoeae adhesin(s) interact with human host cell lutropin receptor on Hec1B cells and appear to trigger a contact inducible uptake. This receptor is selectively expressed by cells in the female urogenital tract
-
Spence JM, Chen JC, Clark VL A proposed role for the lutropin receptor in contact-inducible gonococcal invasion of Hec1B cells. Infect Immun. 65:1997;3736-3742. Unknown N. gonorrhoeae adhesin(s) interact with human host cell lutropin receptor on Hec1B cells and appear to trigger a contact inducible uptake. This receptor is selectively expressed by cells in the female urogenital tract.
-
(1997)
Infect Immun
, vol.65
, pp. 3736-3742
-
-
Spence, J.M.1
Chen, J.C.2
Clark, V.L.3
-
39
-
-
0029061590
-
A lipopolysaccharide-binding site on HepG2 cells similar to the gonococcal opacity-associated surface protein Opa
-
Porat N, Apicella MA, Blake MS A lipopolysaccharide-binding site on HepG2 cells similar to the gonococcal opacity-associated surface protein Opa. Infect Immun. 63:1995;2164-2172.
-
(1995)
Infect Immun
, vol.63
, pp. 2164-2172
-
-
Porat, N.1
Apicella, M.A.2
Blake, M.S.3
-
40
-
-
0024044196
-
Identification of carbohydrate structures that are possbile receptors for Neisseria gonorrhoeae
-
Stromberg N, Deal C, Nyberg G, Normark S, So M, Karlsson K Identification of carbohydrate structures that are possbile receptors for Neisseria gonorrhoeae. Proc Natl Acad Sci USA. 85:1988;4902-4906.
-
(1988)
Proc Natl Acad Sci USA
, vol.85
, pp. 4902-4906
-
-
Stromberg, N.1
Deal, C.2
Nyberg, G.3
Normark, S.4
So, M.5
Karlsson, K.6
-
41
-
-
0025326184
-
Lacto- And ganglio-series glycolipids are adhesion receptors for Neisseria gonorrhoeae
-
Deal CD, Krivan HC Lacto- and ganglio-series glycolipids are adhesion receptors for Neisseria gonorrhoeae. J Biol Chem. 265:1990;12774-12777.
-
(1990)
J Biol Chem
, vol.265
, pp. 12774-12777
-
-
Deal, C.D.1
Krivan, H.C.2
-
42
-
-
0025022678
-
Identification and characterization of a Neisseria gonorrhoeae gene encoding a glycolipid-binding adhesin
-
Paruchuri DK, Seifert HS, Ajioka RS, Karlsson KA, So M Identification and characterization of a Neisseria gonorrhoeae gene encoding a glycolipid-binding adhesin. Proc Natl Acad Sci USA. 87:1990;333-337.
-
(1990)
Proc Natl Acad Sci USA
, vol.87
, pp. 333-337
-
-
Paruchuri, D.K.1
Seifert, H.S.2
Ajioka, R.S.3
Karlsson, K.A.4
So, M.5
-
43
-
-
0032494145
-
Gonococcal invation of epithelial cells driven by P.IA, a bacterial ion channel with GTP binding properties
-
This paper describes the first time the porin-dependent invasion of N. gonorrhoeae into Chang epithelial cells in the absence of Opa invasins. Invasion is only promoted by the P.IA type of these nucleotide-binding porins and strictly dependent on the absence of phosphate. Phosphate appears to block porin function directly by interfering with the nucleotide binding site
-
Van Putten JPM, Duensing TD, Carlson J Gonococcal invation of epithelial cells driven by P.IA, a bacterial ion channel with GTP binding properties. J Exp Med. 188:1998;941-952. This paper describes the first time the porin-dependent invasion of N. gonorrhoeae into Chang epithelial cells in the absence of Opa invasins. Invasion is only promoted by the P.IA type of these nucleotide-binding porins and strictly dependent on the absence of phosphate. Phosphate appears to block porin function directly by interfering with the nucleotide binding site.
-
(1998)
J Exp Med
, vol.188
, pp. 941-952
-
-
Van Putten, J.P.M.1
Duensing, T.D.2
Carlson, J.3
-
44
-
-
0029996134
-
Gonococcal opacity protein promotes bacterial entry-associated rearrangements of the epithelial cell actin cytoskeleton
-
Grassme HU, Ireland RM, van Putten JPM Gonococcal opacity protein promotes bacterial entry-associated rearrangements of the epithelial cell actin cytoskeleton. Infect Immun. 64:1996;1621-1630.
-
(1996)
Infect Immun
, vol.64
, pp. 1621-1630
-
-
Grassme, H.U.1
Ireland, R.M.2
Van Putten, J.P.M.3
-
45
-
-
0030955850
-
Ultrastructural analysis of primary human urethral epithelial cell cultures infected with Neisseria gonorrhoeae
-
Harvey HA, Ketterer MRr, Preston A, Lubaroff D, Williams R, Apicella MA Ultrastructural analysis of primary human urethral epithelial cell cultures infected with Neisseria gonorrhoeae. Infect Immun. 65:1997;2420-2427.
-
(1997)
Infect Immun
, vol.65
, pp. 2420-2427
-
-
Harvey, H.A.1
Ketterer, M.2
Preston, A.3
Lubaroff, D.4
Williams, R.5
Apicella, M.A.6
-
46
-
-
0031813905
-
Neisseria gonorrhoeae induces focal polymerization of actin in primary human urethral epithelium
-
First description that focal actin recruitment appears in primary human urethral epithelium in response to an infection with N. gonorrhoeae. The observed cytoskeletal reorganisation may have implications for a role of epithelial cell invasion and transcytosis of N. gonorrhoeae in vivo
-
Giardina PC, Williams R, Lubaroff D, Apicella MA Neisseria gonorrhoeae induces focal polymerization of actin in primary human urethral epithelium. Infect Immun. 66:1998;3416-3419. First description that focal actin recruitment appears in primary human urethral epithelium in response to an infection with N. gonorrhoeae. The observed cytoskeletal reorganisation may have implications for a role of epithelial cell invasion and transcytosis of N. gonorrhoeae in vivo.
-
(1998)
Infect Immun
, vol.66
, pp. 3416-3419
-
-
Giardina, P.C.1
Williams, R.2
Lubaroff, D.3
Apicella, M.A.4
-
47
-
-
0030864090
-
- gonococci and meningococci to epithelial cells elicits cortical actin rearrangements and clustering of tyrosine-phosphorylated proteins
-
-), which adhere to cells via the type IV pili. These strains trigger phosphotyrosine phosphorylation of proteins at the sites of bacterial contact
-
-), which adhere to cells via the type IV pili. These strains trigger phosphotyrosine phosphorylation of proteins at the sites of bacterial contact.
-
(1997)
Infect Immun
, vol.65
, pp. 4341-4349
-
-
Merz, A.J.1
So, M.2
-
48
-
-
0032145556
-
Ligation of cell surface heparan sulfate proteoglycans by antibody-coated beads stimulates phagocytic uptake into epithelial cells: A model for cellular invasion by Neisseria gonorrhoeae
-
Use of heparan sulphate proteoglycan (HSPG)-ligating latex particles as a model for epithelial cell invasion by N. gonorrhoeae. Confirmation of vibronectin-stimulated uptake and evidence for a role of protein kinase C (PKC) in HSPG-dependent phagocytosis
-
Dehio C, Freissler E, Lanz C, Gómez-Duarte OG, David G, Meyer TF Ligation of cell surface heparan sulfate proteoglycans by antibody-coated beads stimulates phagocytic uptake into epithelial cells: a model for cellular invasion by Neisseria gonorrhoeae. Exp Cell Res. 242:1998;528-539. Use of heparan sulphate proteoglycan (HSPG)-ligating latex particles as a model for epithelial cell invasion by N. gonorrhoeae. Confirmation of vibronectin-stimulated uptake and evidence for a role of protein kinase C (PKC) in HSPG-dependent phagocytosis.
-
(1998)
Exp Cell Res
, vol.242
, pp. 528-539
-
-
Dehio, C.1
Freissler, E.2
Lanz, C.3
Gómez-Duarte, O.G.4
David, G.5
Meyer, T.F.6
-
49
-
-
0030775369
-
Acidic sphingomyelinase mediates entry of N. gonorrhoeae into nonphagocytic cells
-
First report on the function of acidic sphingomyelinase (ASM) in epithelial cell invasion by a bacterial pathogen. The activity of ASM is increased upon interaction of invasive N. gonorrhoeae with Chang epithelial cells and inhibitors of the ASM pathway reduce invasion. ASM-deficient fibroblasts are not invaded by N. gonorrhoeae, however, genetic complementation of cells by ASM effectively restores invasion
-
Grassme H, Gulbins E, Brenner B, Ferlinz K, Sandhoff K, Harzer K, Lang F, Meyer TF Acidic sphingomyelinase mediates entry of N. gonorrhoeae into nonphagocytic cells. Cell. 91:1997;605-615. First report on the function of acidic sphingomyelinase (ASM) in epithelial cell invasion by a bacterial pathogen. The activity of ASM is increased upon interaction of invasive N. gonorrhoeae with Chang epithelial cells and inhibitors of the ASM pathway reduce invasion. ASM-deficient fibroblasts are not invaded by N. gonorrhoeae, however, genetic complementation of cells by ASM effectively restores invasion.
-
(1997)
Cell
, vol.91
, pp. 605-615
-
-
Grassme, H.1
Gulbins, E.2
Brenner, B.3
Ferlinz, K.4
Sandhoff, K.5
Harzer, K.6
Lang, F.7
Meyer, T.F.8
-
50
-
-
0026776537
-
Human neutrophil response to recombinant neisserial Opa proteins
-
Belland RJ, Chen T, Swanson J, Fischer SH Human neutrophil response to recombinant neisserial Opa proteins. Mol Microbiol. 6:1992;1729-1737.
-
(1992)
Mol Microbiol
, vol.6
, pp. 1729-1737
-
-
Belland, R.J.1
Chen, T.2
Swanson, J.3
Fischer, S.H.4
-
51
-
-
0030765750
-
Differential response of human monocytes to Neisseria gonorrhoeae variants expressing pili and opacity proteins
-
Knepper B, Heuer I, Meyer TF, van Putten JPM Differential response of human monocytes to Neisseria gonorrhoeae variants expressing pili and opacity proteins. Infect Immun. 65:1997;4122-4129.
-
(1997)
Infect Immun
, vol.65
, pp. 4122-4129
-
-
Knepper, B.1
Heuer, I.2
Meyer, T.F.3
Van Putten, J.P.M.4
-
52
-
-
0031053335
-
Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells
-
Beauchemin N, Kunath T, Robitaille J, Chow B, Turbide C, Daniels E, Veillette A Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells. Oncogene. 14:1997;783-790.
-
(1997)
Oncogene
, vol.14
, pp. 783-790
-
-
Beauchemin, N.1
Kunath, T.2
Robitaille, J.3
Chow, B.4
Turbide, C.5
Daniels, E.6
Veillette, A.7
-
53
-
-
0027185152
-
T cell activation by clustered tyrosine kinases
-
Kolanus W, Romeo C, Seed B T cell activation by clustered tyrosine kinases. Cell. 74:1993;171-183.
-
(1993)
Cell
, vol.74
, pp. 171-183
-
-
Kolanus, W.1
Romeo, C.2
Seed, B.3
-
54
-
-
0008900035
-
Human and mouse killer-cell inhibitory receptors recruit PTP1C and PTP1D protein tyrosine phosphatases
-
Olcese L, Lang P, Vely F, Cambiaggi A, Marguet D, Blery M, Hippen KL, Biassoni R, Moretta A, Moretta Let al. Human and mouse killer-cell inhibitory receptors recruit PTP1C and PTP1D protein tyrosine phosphatases. J Immunol. 156:1996;4531-4534.
-
(1996)
J Immunol
, vol.156
, pp. 4531-4534
-
-
Olcese, L.1
Lang, P.2
Vely, F.3
Cambiaggi, A.4
Marguet, D.5
Blery, M.6
Hippen, K.L.7
Biassoni, R.8
Moretta, A.9
Moretta, L.10
-
55
-
-
0028859572
-
CD66 family members are associated with tyrosine kinase activity in human neutrophils
-
Skubitz KM, Campbell KD, Ahmed K, Skubitz AP CD66 family members are associated with tyrosine kinase activity in human neutrophils. J Immunol. 155:1995;5382-5390.
-
(1995)
J Immunol
, vol.155
, pp. 5382-5390
-
-
Skubitz, K.M.1
Campbell, K.D.2
Ahmed, K.3
Skubitz, A.P.4
-
56
-
-
0032518818
-
CD66-mediated phagocytosis of Opa52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase- And Rac1-dependent signalling pathway
-
52 bacteria, indicating a crucial role of this signalling for the opsonin-independent Opa52/CD66-mediated phagocytosis of pathogenic N. gonorrhoeae
-
52 bacteria, indicating a crucial role of this signalling for the opsonin-independent Opa52/CD66-mediated phagocytosis of pathogenic N. gonorrhoeae.
-
(1998)
EMBO J
, vol.17
, pp. 443-454
-
-
Hauck, C.R.1
Meyer, T.F.2
Lang, F.3
Gulbins, E.4
-
57
-
-
1842287946
-
Neisseria gonorrhoeae epithelial cell interaction leads to the activation of the transcription factors nuclear factor kappaB and activator protein 1 and the induction of inflammatory cytokines
-
The first report on the contact-dependent induction of proinflammatory cytokines upon contact of N. gonorrhoeae with epithelial cells. The upregulation of the cytokine/chemokine genes involves the activity of the transcription factors NF-κB and AP-1. Induction of these immune response mediators is serum-independent and take place by N. gonorrhoeae strains expressing either Opa or pili
-
Naumann M, Wessler S, Bartsch C, Wieland B, Meyer TF Neisseria gonorrhoeae epithelial cell interaction leads to the activation of the transcription factors nuclear factor kappaB and activator protein 1 and the induction of inflammatory cytokines. J Exp Med. 186:1997;247-258. The first report on the contact-dependent induction of proinflammatory cytokines upon contact of N. gonorrhoeae with epithelial cells. The upregulation of the cytokine/chemokine genes involves the activity of the transcription factors NF-κB and AP-1. Induction of these immune response mediators is serum-independent and take place by N. gonorrhoeae strains expressing either Opa or pili.
-
(1997)
J Exp Med
, vol.186
, pp. 247-258
-
-
Naumann, M.1
Wessler, S.2
Bartsch, C.3
Wieland, B.4
Meyer, T.F.5
-
58
-
-
0029043830
-
Inflammatory cytokines produced in response to experimental human gonorrhea
-
Ramsey KH, Schneider H, Cross AS, Boslego JW, Hoover DL, Staley TL, Kuschner RA, Deal CD Inflammatory cytokines produced in response to experimental human gonorrhea. J Infect Dis. 172:1995;186-191.
-
(1995)
J Infect Dis
, vol.172
, pp. 186-191
-
-
Ramsey, K.H.1
Schneider, H.2
Cross, A.S.3
Boslego, J.W.4
Hoover, D.L.5
Staley, T.L.6
Kuschner, R.A.7
Deal, C.D.8
-
59
-
-
0032487573
-
Coordinate activation of activator protein 1 and inflammatory cytokines in response to Neisseria gonorrhoeae epithelial cell contact involves stress response kinases
-
This paper demonstrates that the signalling leading to the activation of the transcription factor AP-1 in response to N. gonorrhoeae-epithelial cell contact involves GTPases and stress response kinases PAK, MKK4 and JNK
-
Naumann M, Rudel T, Wieland B, Bartsch C, Meyer TF Coordinate activation of activator protein 1 and inflammatory cytokines in response to Neisseria gonorrhoeae epithelial cell contact involves stress response kinases. J Exp Med. 188:1998;1277-1286. This paper demonstrates that the signalling leading to the activation of the transcription factor AP-1 in response to N. gonorrhoeae-epithelial cell contact involves GTPases and stress response kinases PAK, MKK4 and JNK.
-
(1998)
J Exp Med
, vol.188
, pp. 1277-1286
-
-
Naumann, M.1
Rudel, T.2
Wieland, B.3
Bartsch, C.4
Meyer, T.F.5
-
60
-
-
0030875602
-
MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42
-
Fanger GR, Johnson NL, Johnson GL MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42. EMBO J. 16:1997;4961-4972.
-
(1997)
EMBO J
, vol.16
, pp. 4961-4972
-
-
Fanger, G.R.1
Johnson, N.L.2
Johnson, G.L.3
-
61
-
-
0029054398
-
Glucosylation of Rho proteins by Clostridium difficile toxin B
-
Just I, Selzer J, Wilm M, Von ES, Mann M, Aktories K Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature. 375:1995;500-503.
-
(1995)
Nature
, vol.375
, pp. 500-503
-
-
Just, I.1
Selzer, J.2
Wilm, M.3
Von, E.S.4
Mann, M.5
Aktories, K.6
-
63
-
-
0025861823
-
Effects of protein I of Neisseria gonorrhoeae on neutrophil activation: Generation of diacylglycerol from phosphatidylcholine via a specific phospholipase C is associated with exocytosis
-
Haines KA, Reibman J, Tang XY, Blake M, Weissmann G Effects of protein I of Neisseria gonorrhoeae on neutrophil activation: generation of diacylglycerol from phosphatidylcholine via a specific phospholipase C is associated with exocytosis. J Cell Biol. 114:1991;433-442.
-
(1991)
J Cell Biol
, vol.114
, pp. 433-442
-
-
Haines, K.A.1
Reibman, J.2
Tang, X.Y.3
Blake, M.4
Weissmann, G.5
-
64
-
-
0028861527
-
Neisserial porins inhibit human neutrophil actin polymerization, degranulation, opsonin receptor expression, and phagocytosis but prime the neutrophils to increase their oxidative burst
-
Bjerknes R, Guttormsen HK, Solberg CO, Wetzler LM Neisserial porins inhibit human neutrophil actin polymerization, degranulation, opsonin receptor expression, and phagocytosis but prime the neutrophils to increase their oxidative burst. Infect Immun. 63:1995;160-167.
-
(1995)
Infect Immun
, vol.63
, pp. 160-167
-
-
Bjerknes, R.1
Guttormsen, H.K.2
Solberg, C.O.3
Wetzler, L.M.4
-
65
-
-
0032930533
-
Mutagenesis of the Neisseria gonorrhoeae porin reduces invasion in epithelial cells and increases uptake by phagocytes
-
in press
-
Bauer FJ, Rudel T, Stein M, Meyer TF: Mutagenesis of the Neisseria gonorrhoeae porin reduces invasion in epithelial cells and increases uptake by phagocytes. Mol Microbiol 1998, 31:in press.
-
(1998)
Mol Microbiol
, pp. 31
-
-
Bauer, F.J.1
Rudel, T.2
Stein, M.3
Meyer, T.F.4
-
66
-
-
0032567418
-
Neisseria gonorrhoeae porin modulates phagosome maturation
-
The results of this study indicate that N. gonorrhoeae porin induces changes in the protein composition of phagosomes. Phagocytosis of latex beads in the presence of purified porin by human macrophages leads to a transient increase of annexin II, the early endocytic marker Rab5 and the transferrin receptor and a decrease of the late endocytic marker Rab7 and cathepsin D. Hence, N. gonorrhoeae porin may have the capacity to arrest phagosome maturation within macrophages
-
Mosleh IM, Huber LA, Steinlein P, Pasquali C, Günther D, Meyer TF Neisseria gonorrhoeae porin modulates phagosome maturation. J Biol Chem. 273:1998;35332-35338. The results of this study indicate that N. gonorrhoeae porin induces changes in the protein composition of phagosomes. Phagocytosis of latex beads in the presence of purified porin by human macrophages leads to a transient increase of annexin II, the early endocytic marker Rab5 and the transferrin receptor and a decrease of the late endocytic marker Rab7 and cathepsin D. Hence, N. gonorrhoeae porin may have the capacity to arrest phagosome maturation within macrophages.
-
(1998)
J Biol Chem
, vol.273
, pp. 35332-35338
-
-
Mosleh, I.M.1
Huber, L.A.2
Steinlein, P.3
Pasquali, C.4
Günther, D.5
Meyer, T.F.6
-
67
-
-
0026348619
-
Fate of the major outer membrane protein P.IA in early and late events of gonococcal infection of epithelial cells
-
Weel F, van Putten JPM Fate of the major outer membrane protein P.IA in early and late events of gonococcal infection of epithelial cells. Res Microbiol. 142:1991;985-993.
-
(1991)
Res Microbiol
, vol.142
, pp. 985-993
-
-
Weel, F.1
Van Putten, J.P.M.2
-
68
-
-
0029954217
-
Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: Parallels between pathogen accommodation and mitochondrial endosymbiosis
-
Rudel T, Schmid A, Benz R, Kolb HA, Lang F, Meyer TF Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: parallels between pathogen accommodation and mitochondrial endosymbiosis. Cell. 85:1996;391-402.
-
(1996)
Cell
, vol.85
, pp. 391-402
-
-
Rudel, T.1
Schmid, A.2
Benz, R.3
Kolb, H.A.4
Lang, F.5
Meyer, T.F.6
-
69
-
-
0344142375
-
Neisserial porin (PorB) causes rapid calcium influx in target cells and induces apoptosis by the activation of cysteine proteases
-
in press. First description that N. gonorrhoeae causes apoptosis in epithelial and phagocytic cells. The authors provide evidence that neisserial porin induces an apoptotic mechanism in target cells by causing a rapid and transient increase in cytosolic calcium, followed by the activation of the calcium-dependent cysteine protease calpain and the central apoptosis-executing molecules, the capsases.
-
Müller A, Günther D, Düx F, Naumann M, Meyer TF, Rudel T Neisserial porin (PorB) causes rapid calcium influx in target cells and induces apoptosis by the activation of cysteine proteases. EMBO J. 18:1999;. in press. First description that N. gonorrhoeae causes apoptosis in epithelial and phagocytic cells. The authors provide evidence that neisserial porin induces an apoptotic mechanism in target cells by causing a rapid and transient increase in cytosolic calcium, followed by the activation of the calcium-dependent cysteine protease calpain and the central apoptosis-executing molecules, the capsases.
-
(1999)
EMBO J
, vol.18
-
-
Müller, A.1
Günther, D.2
Düx, F.3
Naumann, M.4
Meyer, T.F.5
Rudel, T.6
-
70
-
-
0029125701
-
Protease activation during apoptosis: Death by a thousand cuts?
-
Martin SJ, Green DR Protease activation during apoptosis: death by a thousand cuts? Cell. 82:1995;349-352.
-
(1995)
Cell
, vol.82
, pp. 349-352
-
-
Martin, S.J.1
Green, D.R.2
-
71
-
-
0030759230
-
Neisserial porins may provide critical second signals to polysaccharide-activated murine B cells for induction of immunoglobulin secretion
-
Snapper CM, Rosas FR, Kehry MR, Mond JJ, Wetzler LM Neisserial porins may provide critical second signals to polysaccharide-activated murine B cells for induction of immunoglobulin secretion. Infect Immun. 65:1997;3203-3208.
-
(1997)
Infect Immun
, vol.65
, pp. 3203-3208
-
-
Snapper, C.M.1
Rosas, F.R.2
Kehry, M.R.3
Mond, J.J.4
Wetzler, L.M.5
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