T4SS ID	35
Strain	Helicobacter pylori P12
Replicon	chromosome [Browse all T4SS(s) in this replicon]
Accession	NC_011498
Location	553525..584777
Name	Cag
Function	effector translocation
Classification	Type IVA; Type P
Experimental investigation has been performed on this T4SS.

T4SS components

Component	CagC	CagD	CagE	CagF	CagG	CagH	CagI	CagL	CagN
Number	1	1	1	1	1	1	1	1	1
Component	CagM	CagT	CagU	CagV	CagW	CagX	CagY	CagZ	Cagalpha
Number	1	1	1	1	1	1	1	1	1
Component	Cagbeta	Caggamma	Cagdelta
Number	1	1	1

The information of T4SS components from NC_011498
#	Locus tag (Gene)	Coordinates [+/-], size (bp)	Protein GI	Product	Component
1	HPP12_0523 (era)	549537..550442 [+], 906	210134718	GTP-binding protein Era
2	HPP12_0524	550439..551431 [+], 993	210134719	hypothetical protein
3	HPP12_0525	551520..552374 [-], 855	210134720	hypothetical protein
4	HPP12_0526	552393..552584 [+], 192	210134721	hypothetical protein
5	HPP12_0527 (cag1)	552705..553052 [+], 348	210134722	cag pathogenicity island protein Zeta
6	HPP12_0528 (cag2)	553160..553525 [+], 366	210134723	cag pathogenicity island protein Epsilon
7	HPP12_0529 (cag3)	553525..554970 [+], 1446	210134724	cag pathogenicity island protein Delta	Cagdelta
8	HPP12_0530 (cag4)	554980..555489 [+], 510	210134725	cag pathogenicity island protein Gamma	Caggamma
9	HPP12_0531 (cag5)	555963..558209 [-], 2247	210134726	cag pathogenicity island protein Beta	Cagbeta
10	HPP12_0532 (virB11-2)	558218..559210 [-], 993	210134727	cag pathogenicity island protein Alpha	Cagalpha
11	HPP12_0533 (cagZ)	559215..559814 [-], 600	210134728	cag pathogenicity island protein Z	CagZ
12	HPP12_0534 (cagY)	559964..565669 [-], 5706	210134729	cag pathogenicity island protein Y VirB10-like protein	CagY
13	HPP12_0535 (cagX)	565684..567252 [-], 1569	210134730	cag pathogenicity island protein X VirB9-like protein	CagX
14	HPP12_0536 (cagW)	567305..568912 [-], 1608	210134731	cag pathogenicity island protein W	CagW
15	HPP12_0537 (cagV)	568917..569675 [-], 759	210134732	cag pathogenicity island protein V	CagV
16	HPP12_0538 (cagU)	570070..570720 [+], 651	210134733	cag pathogenicity island protein U	CagU
17	HPP12_0539 (cagT)	570733..571575 [+], 843	210134734	cag pathogenicity island protein T	CagT
18	HPP12_0540 (cagS)	571777..572376 [-], 600	210134735	cag pathogenicity island protein S
19	HPP12_0541 (cagQ)	572815..573195 [-], 381	210134736	cag pathogenicity island protein Q
20	HPP12_0542 (cagR)	572903..573205 [+], 303	210134737	cag pathogenicity island protein R
21	HPP12_0543 (cagP)	573621..573974 [-], 354	210134738	cag pathogenicity island protein P
22	HPP12_0544 (cagM)	574409..575539 [+], 1131	210134739	cag pathogenicity island protein M	CagM
23	HPP12_0545 (cagN)	575554..576474 [+], 921	210134740	cag pathogenicity island protein N	CagN
24	HPP12_0546 (cagL)	576555..577268 [-], 714	210134741	cag pathogenicity island protein L	CagL
25	HPP12_0547 (cagI)	577265..578410 [-], 1146	210134742	cag pathogenicity island protein I	CagI
26	HPP12_0548 (cagH)	578421..579533 [-], 1113	210134743	cag pathogenicity island protein H	CagH
27	HPP12_0549 (cagG)	579550..579978 [-], 429	210134744	cag pathogenicity island protein G	CagG
28	HPP12_0550 (cagF)	580037..580843 [-], 807	210134745	cag pathogenicity island protein F	CagF
29	HPP12_0551 (cagE)	580845..583796 [-], 2952	210134746	cag pathogenicity island protein E VirB4-like protein	CagE
30	HPP12_0552 (cagD)	583805..584428 [-], 624	210134747	cag pathogenicity island protein D	CagD
31	HPP12_0553 (cagC)	584430..584777 [-], 348	210134748	cag pathogenicity island protein C	CagC
32	HPP12_0554 (cagB)	584923..585150 [-], 228	210134749	cag pathogenicity island protein B
33	HPP12_0555 (cagA)	585581..589225 [+], 3645	210134750	cytotoxin-associated protein A

 This T4SS contains information of accessory protein.
 This T4SS contains information of interaction.

Genes in the 5-Kb flanking regions if available, or non-essential genes in the T4SS gene cluster if any.

Download FASTA format files

Proteins        Genes

Effectors

CagA; Peptidoglycan

The information of protein effectors
#	Locus tag (Gene)	Coordinates [+/-], size (bp)	Protein GI	Product	*
1	HPP12_0555 (cagA)	585581..589225 [+], 3645	210134750	cytotoxin-associated protein A	CagA

 T4SE derived from experimental literature.
 This effector contains information of interaction.

Download FASTA format files

Proteins        Genes

The information on requirements for T4SS substrate-channel docking

Certain T4SS substrates require secretion chaperones for translocation. These chaperones often possess physical properties (small size of 15 kDa, acidic pI, and amphipathic helices) resembling those of chaperones associated with the type III secretion systems, a family of macromolecular translocation systems ancestrally related to bacterial flagella.

#	Accessory protein(GI)	motif(s)	Substrate(s)	Function	Reference
1	CagF (chaperone) (210134745)	CT20aa and an intact N terminus	CagA	The CagA-binding protein CagF is a secretion chaperone-like protein that interacts with a 100 aa region that is adjacent to the C-terminal secretion signal of CagA.CagF is a translocation factor for CagA, but is not translocated by the type IV apparatus.	(1) PubMed: 17768234

Tips:
1.Substrate(s): For the conjugation systems, the listed proteins are relaxases that bind a cognate T4CP and are delivered to recipient cells. For the effector translocator systems, the listed proteins are effectors that play a role in the infection processes of the bacterial pathogen.
2.motif(s):The motifs listed are required for substrate translocation. In some cases, the protein or its C-terminal fragment (CT) is sufficient to mediate translocation to target cells, as shown by fusion to a reporter protein such as Cre recombinase or adenylate cyclase. Amino acids (aa) at positions listed relative to the C-terminal fragment (subscript) are required for translocation, as shown by mutational analysis. ND, not determined. Parentheses indicate that the interaction between a protein substrate and a cognate T4CP has been experimentally shown.
3.Accessory protein: Accessory factors required for T4SS channel docking or translocation. The proposed function in mediating substrate-T4SS channel docking is shown in parentheses.PubMed:19946141

(1) Pattis I; Weiss E; Laugks R; Haas R; Fischer W (2007). The Helicobacter pylori CagF protein is a type IV secretion chaperone-like molecule that binds close to the C-terminal secretion signal of the CagA effector protein. Microbiology. 153(Pt 9):2896-909. [PudMed:17768234]

The information on host-pathogen interaction.

#	Name(Protein GI)	Host site/Substrate	Source	Function	Reference
1	CagA (210134750)	SHP-2	human	CagA is translocated into gastric epithelial cells. It physically interacts with SHP-2 to modify cellular functions and perturb mammalian signal transduction machineries. This may induce gastric epithelial cells to move and proliferate abnormally and help to acquire a cellular transformed phenotype.	(1) PubMed: 11743164
2	CagA (210134750)	growth factor receptor bound 2 (Grb2)	unknown	CagA targets to Grb2 and this process leads to activing the MEK/ERK pathway and results in cell scattering and proliferation.	(2) PubMed: 12419219
3	CagA (210134750)	PAR1/MARK kinase	human	CagA interacts with PAR1/MARK kinase to inhibit the activity of PAR1 kinase and prevent PAR1 phosphorylation which mediated by atypical protein kinase C (aPKC).	(3) PubMed: 17507984
4	CagA (210134750)	Apoptosis-stimulating of p53 protein 2 (ASPP2)	human	ASPP2 is a tumor suppressor that activates the apoptotic response upon cellular stress which mediated by p53. CagA interacts with ASPP2 to change the function of ASPP2 and this process leads to the decreased survival of cells which infected by H. pylori.	(4) PubMed: 24474782
5	CagA (210134750)	protein kinase C-related kinase 2 (PRK2)	human	CagA represses kinase activity of PRK2, which has been involved in establishment of cell polarity and rearrangements of cytoskeleton, to further control signalling pathways associated with cancer.	(5) PubMed: 26041307
6	CagA (210134750)	Glycogen synthase kinase 3 (GSK-3)	human	CagA interacts with GSK-3 to reduce its activity by cause it to transform into an insoluble fraction. CagA then induce a epithelial mesenchymal transition mediated by Snail via the comsuming of GSK-3.	(6) PubMed: 25055241
7	CagA (210134750)	c-Met	human	CagA interacts with the c-Met receptor to modulates cellular functions through deregulating c-Met receptor signaling and participates in invasive growth of tumor cells.	(7) PubMed: 12719469
8	CagA (210134750)	E-cadherin	human	CagA interacts with E-cadherin to impair the complex formation between E-cadherin and beta-catenin and facilitate transdifferentiation of intestines in gastric epithelial cells.	(8) PubMed: 17237808
9	CagA (210134750)	host membrane phosphatidylserine	unknown	CagA can be tethered to the inner leaflet of the plasma membrane by interacting with phosphatidylserine. Then it binds the PAR1/MARK to induce polarity and junctional defects.	(9) PubMed: 20478541
10	CagA (210134750)	c-Abl tyrosine kinase	human	CagA targets to c-Abl directly and localizes in focal adhesion complexes and membrane ruffles.	(10) PubMed: 17160020
11	CagA (210134750)	αPix	human	CagA interacted with αPix to activates PAK1, ERK and NF-kappaB after being delivered into AGS cells. Then it induces the expression of IL-8 in infected gastric epithelial cells.	(11) PubMed: 19672789
12	CagA (210134750)	scaffolding protein ZO-1	human, canine	CagA interacts with epithelial tight-junction ZO-1 and the transmembrane protein junctional adhesion molecule to change the function and composition of the apical-junctional complex.	(12) PubMed: 12775840
13	CagA (210134750)	integrin α5β1 receptor	human	CagA binds interface with α5β1 integrin.It is an essential step for the translocation process of CagA into the host cell.	(13) PubMed: 22908298
14	CagA (210134750)	TNF receptor-associated factor 1 and 4-1BB (TRAF1 and 4-1BB)	human	CagA facilitates the proliferation and represses the apoptosis of GES-1 cells by upregulated TRAF1/4-1BB.	(14) PubMed: 28627614
15	CagA (210134750)	Adapter molecule crk	human	The interaction between CagA and Crk adaptor proteins is important for loss of gastric epithelial cell adhesion induced by Helicobacter pylori-induced Helicobacter pylori.	(15) PubMed: 16275761
16	CagA (210134750)	SHP-1	human	CagA interacts with SHP1 to enhance the phosphatase activity of SHP1 so that it dampens the oncogenic action of CagA.	(16) PubMed: 27572445
17	CagA (210134750)	Transforming growth factor-beta-activated kinase 1 (TAK1)	human	CagA interacts with TAK1 and improves its activity to activate NF-kappaB through the ubiquitination of TAK1.	(17) PubMed: 19820695
18	CagA (210134750)	Myeloid cell leukemia sequence-1 (MCL1)	mongolian gerbil	CagA increases MCL1 thorough the interaction between SRE/SRF and CagA/MCL1 in modulating rapid turnover of pit epithelial cells via MEK/ERK/SRE activation.	(18) PubMed: 18005743
19	CagL (210134741)	integrin α5β1 receptor	human	CagL, which is targeted to the pilus surface, is a specialized adhesin. It binds to and activates integrin α5β1 receptor on gastric epithelial cells. This interaction triggers CagA delivery into target cells.	(19) PubMed: 17943123
20	CagL (210134741)	integrin αvβ3	human	Host cell docking of T4SS.	(20) PubMed: 21915696
21	CagL (210134741)	integrin αvβ5	human	CagL/integrin β5 signalling complex is important for gastrin expression induced by H. pylori.	(21) PubMed: 22287591
22	CagL (210134741)	integrin αvβ6	human	αvβ6 is a specific, high affinity receptor for CagL.	(22) PubMed: 31197920
23	CagY (210134729)	integrin α5β1 receptor	human	CagY interacts with α5β1 integrin, which acts like a molecular rheostat that modulates the host immune response to facilitate persistent infection.	(23) PubMed: 29764950

This T4SE is mentioned in the literature.
This T4SE is highly identical with the protein mentioned in the literature.

(1) Higashi H et al. (2002). SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. Science. 295(5555):683-6. [PudMed:11743164]

(2) Mimuro H et al. (2002). Grb2 is a key mediator of helicobacter pylori CagA protein activities. Mol Cell. 10(4):745-55. [PudMed:12419219]

(3) Saadat I et al. (2007). Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity. Nature. 447(7142):330-3. [PudMed:17507984]

(4) Nešić D et al. (2014). Structure of the Helicobacter pylori CagA oncoprotein bound to the human tumor suppressor ASPP2. Proc Natl Acad Sci U S A. 111(4):1562-7. [PudMed:24474782]

(5) Mishra JP et al. (2015). CagA of Helicobacter pylori interacts with and inhibits the serine-threonine kinase PRK2. Cell Microbiol. 17(11):1670-82. [PudMed:26041307]

(6) Lee DG et al. (2014). Helicobacter pylori CagA promotes Snail-mediated epithelial-mesenchymal transition by reducing GSK-3 activity. Nat Commun. 5:4423. [PudMed:25055241]

(7) Churin Y et al. (2003). Helicobacter pylori CagA protein targets the c-Met receptor and enhances the motogenic response. J Cell Biol. 161(2):249-55. [PudMed:12719469]

(8) Murata-Kamiya N et al. (2007). Helicobacter pylori CagA interacts with E-cadherin and deregulates the beta-catenin signal that promotes intestinal transdifferentiation in gastric epithelial cells. Oncogene. 26(32):4617-26. [PudMed:17237808]

(9) Murata-Kamiya N; Kikuchi K; Hayashi T; Higashi H; Hatakeyama M (2010). Helicobacter pylori exploits host membrane phosphatidylserine for delivery, localization, and pathophysiological action of the CagA oncoprotein. Cell Host Microbe. 7(5):399-411. [PudMed:20478541]

(10) Poppe M; Feller SM; Romer G; Wessler S (2007). Phosphorylation of Helicobacter pylori CagA by c-Abl leads to cell motility. Oncogene. 26(24):3462-72. [PudMed:17160020]

(11) Lim JW et al. (2009). alphaPix interacts with Helicobacter pylori CagA to induce IL-8 expression in gastric epithelial cells. Scand J Gastroenterol. 44(10):1166-72. [PudMed:19672789]

(12) Amieva MR et al. (2003). Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA. Science. 300(5624):1430-4. [PudMed:12775840]

(13) Kaplan-Türköz B et al. (2012). Structural insights into Helicobacter pylori oncoprotein CagA interaction with β1 integrin. Proc Natl Acad Sci U S A. 109(36):14640-5. [PudMed:22908298]

(14) Wang F et al. (2017). CagA promotes proliferation and inhibits apoptosis of GES-1 cells by upregulating TRAF1/4-1BB. Mol Med Rep. 16(2):1262-1268. [PudMed:28627614]

(15) Suzuki M et al. (2005). Interaction of CagA with Crk plays an important role in Helicobacter pylori-induced loss of gastric epithelial cell adhesion. J Exp Med. 202(9):1235-47. [PudMed:16275761]

(16) Saju P et al. (2016). Host SHP1 phosphatase antagonizes Helicobacter pylori CagA and can be downregulated by Epstein-Barr virus. Nat Microbiol. 1:16026. [PudMed:27572445]

(17) Lamb A et al. (2009). Helicobacter pylori CagA activates NF-kappaB by targeting TAK1 for TRAF6-mediated Lys 63 ubiquitination. EMBO Rep. 10(11):1242-9. [PudMed:19820695]

(18) Mimuro H et al. (2007). Helicobacter pylori dampens gut epithelial self-renewal by inhibiting apoptosis, a bacterial strategy to enhance colonization of the stomach. Cell Host Microbe. 2(4):250-63. [PudMed:18005743]

(19) Kwok T; Zabler D; Urman S; Rohde M; Hartig R; Wessler S; Misselwitz R; Berger J; Sewald N; Konig W; Backert S (2007). Helicobacter exploits integrin for type IV secretion and kinase activation. Nature. 449(7164):862-6. [PudMed:17943123]

(20) Conradi J; Huber S; Gaus K; Mertink F; Royo Gracia S; Strijowski U; Backert S; Sewald N (2012). Cyclic RGD peptides interfere with binding of the Helicobacter pylori protein CagL to integrins alpha(V)beta (3) and alpha (5)beta (1). Amino Acids. 43(1):219-32. [PudMed:21915696]

(21) Wiedemann T et al. (2012). Helicobacter pylori CagL dependent induction of gastrin expression via a novel αvβ5-integrin-integrin linked kinase signalling complex. Gut. 61(7):986-96. [PudMed:22287591]

(22) Buß M et al. (2019). Specific high affinity interaction of Helicobacter pylori CagL with integrin αV β6 promotes type IV secretion of CagA into human cells. FEBS J. . [PudMed:31197920]

(23) Skoog EC et al. (2018). CagY-Dependent Regulation of Type IV Secretion in Helicobacter pylori Is Associated with Alterations in Integrin Binding. MBio. 9(3). pii: e00717-18. [PudMed:29764950]

(1) You Y; He L; Zhang M; Fu J; Gu Y; Zhang B; Tao X; Zhang J (2012). Comparative Genomics of Helicobacter pylori Strains of China Associated with Different Clinical Outcome. PLoS One. 7(6):e38528. [PudMed:22701658]

(2) Koch M; Mollenkopf HJ; Klemm U; Meyer TF (2012). Induction of microRNA-155 is TLR- and type IV secretion system-dependent in macrophages and inhibits DNA-damage induced apoptosis. Proc Natl Acad Sci U S A. 109(19):E1153-62. [PudMed:22509021]

(3) Pham KT; Weiss E; Jimenez Soto LF; Breithaupt U; Haas R; Fischer W (2012). CagI is an essential component of the Helicobacter pylori Cag type IV secretion system and forms a complex with CagL. PLoS One. 7(4):e35341. [PudMed:22493745]

(4) Jimenez-Soto LF; Rohrer S; Jain U; Ertl C; Sewald X; Haas R (2012). Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro. Helicobacter. 17(2):133-9. [PudMed:22404444]

(5) Backert S; Clyne M; Tegtmeyer N (2011). Molecular mechanisms of gastric epithelial cell adhesion and injection of CagA by Helicobacter pylori. Cell Commun Signal. 9:28. [PudMed:22044679]

(6) Kumar Pachathundikandi S; Brandt S; Madassery J; Backert S (2011). Induction of TLR-2 and TLR-5 expression by Helicobacter pylori switches cagPAI-dependent signalling leading to the secretion of IL-8 and TNF-alpha. PLoS One. 6(5):e19614. [PudMed:21573018]

(7) Schneider S; Carra G; Sahin U; Hoy B; Rieder G; Wessler S (2011). Complex cellular responses of Helicobacter pylori-colonized gastric adenocarcinoma cells. Infect Immun. 79(6):2362-71. [PudMed:21402757]

(8) Tegtmeyer N; Backert S (2011). Role of Abl and Src family kinases in actin-cytoskeletal rearrangements induced by the Helicobacter pylori CagA protein. Eur J Cell Biol. 90(11):880-90. [PudMed:21247656]

(9) Fischer W; Windhager L; Rohrer S; Zeiller M; Karnholz A; Hoffmann R; Zimmer R; Haas R (2010). Strain-specific genes of Helicobacter pylori: genome evolution driven by a novel type IV secretion system and genomic island transfer. Nucleic Acids Res. 38(18):6089-101. [PudMed:20478826]

(10) Saha A; Backert S; Hammond CE; Gooz M; Smolka AJ (2010). Helicobacter pylori CagL activates ADAM17 to induce repression of the gastric H, K-ATPase alpha subunit. Gastroenterology. 139(1):239-48. [PudMed:20303353]

(11) Fehri LF; Rechner C; Janssen S; Mak TN; Holland C; Bartfeld S; Bruggemann H; Meyer TF (2009). Helicobacter pylori-induced modification of the histone H3 phosphorylation status in gastric epithelial cells reflects its impact on cell cycle regulation. Epigenetics. 4(8):577-86. [PudMed:20081355]

(12) Jimenez-Soto LF; Kutter S; Sewald X; Ertl C; Weiss E; Kapp U; Rohde M; Pirch T; Jung K; Retta SF; Terradot L; Fischer W; Haas R (2009). Helicobacter pylori type IV secretion apparatus exploits beta1 integrin in a novel RGD-independent manner. PLoS Pathog. 5(12):e1000684. [PudMed:19997503]

(13) Brandt S; Wessler S; Hartig R; Backert S (2009). Helicobacter pylori activates protein kinase C delta to control Raf in MAP kinase signalling: role in AGS epithelial cell scattering and elongation. Cell Motil Cytoskeleton. 66(10):874-92. [PudMed:19437514]

(14) Svensson H; Hansson M; Kilhamn J; Backert S; Quiding-Jarbrink M (2009). Selective upregulation of endothelial E-selectin in response to Helicobacter pylori-induced gastritis. Infect Immun. 77(7):3109-16. [PudMed:19414551]

(15) Hare S; Fischer W; Williams R; Terradot L; Bayliss R; Haas R; Waksman G (2007). Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase. EMBO J. 26(23):4926-34. [PudMed:17972918]

(16) Kwok T; Zabler D; Urman S; Rohde M; Hartig R; Wessler S; Misselwitz R; Berger J; Sewald N; Konig W; Backert S (2007). Helicobacter exploits integrin for type IV secretion and kinase activation. Nature. 449(7164):862-6. [PudMed:17943123]

(17) Pattis I; Weiss E; Laugks R; Haas R; Fischer W (2007). The Helicobacter pylori CagF protein is a type IV secretion chaperone-like molecule that binds close to the C-terminal secretion signal of the CagA effector protein. Microbiology. 153(Pt 9):2896-909. [PudMed:17768234]

(18) Poppe M; Feller SM; Romer G; Wessler S (2007). Phosphorylation of Helicobacter pylori CagA by c-Abl leads to cell motility. Oncogene. 26(24):3462-72. [PudMed:17160020]

(19) Garcia JT; Ferracci F; Jackson MW; Joseph SS; Pattis I; Plano LR; Fischer W; Plano GV (2006). Measurement of effector protein injection by type III and type IV secretion systems by using a 13-residue phosphorylatable glycogen synthase kinase tag. Infect Immun. 74(10):5645-57. [PudMed:16988240]

(20) Backert S; Kwok T; Konig W (2005). Conjugative plasmid DNA transfer in Helicobacter pylori mediated by chromosomally encoded relaxase and TraG-like proteins. Microbiology. 151(Pt 11):3493-503. [PudMed:16272373]

(21) Bauer B; Moese S; Bartfeld S; Meyer TF; Selbach M (2005). Analysis of cell type-specific responses mediated by the type IV secretion system of Helicobacter pylori. Infect Immun. 73(8):4643-52. [PudMed:16040977]

(22) Wessler S; Rapp UR; Wiedenmann B; Meyer TF; Schoneberg T; Hocker M; Naumann M (2002). B-Raf/Rap1 signaling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection. FASEB J. 16(3):417-9. [PudMed:11790728]

(23) Churin Y; Kardalinou E; Meyer TF; Naumann M (2001). Pathogenicity island-dependent activation of Rho GTPases Rac1 and Cdc42 in Helicobacter pylori infection. Mol Microbiol. 40(4):815-23. [PudMed:11401689]

(24) Stein M; Rappuoli R; Covacci A; Blanke SR; Ye D; Odenbreit S; Gebert B; Puls J; Fischer W; Haas R (2001). Interaction of Helicobacter pylori with professional phagocytes: role of the cag pathogenicity island and translocation, phosphorylation and processing of CagA. Cell Microbiol. 3(1):21-31. [PudMed:11207617]

(25) Ramarao N; Gray-Owen SD; Backert S; Meyer TF (2000). Helicobacter pylori inhibits phagocytosis by professional phagocytes involving type IV secretion components. Mol Microbiol. 37(6):1389-404. [PudMed:10998171]

(26) Odenbreit S; Puls J; Sedlmaier B; Gerland E; Fischer W; Haas R (2000). Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion. Science. 287(5457):1497-500. [PudMed:10688800]

This literature contains experimental investigation

This literature contains bioinformatics investigation