Neisserial porin (PorB) causes rapid calcium influx in target cells and induces apoptosis by the activation of cysteine proteases.

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  • Additional Information
    • Source:
      Publisher: Nature Publishing Group Country of Publication: England NLM ID: 8208664 Publication Model: Print Cited Medium: Print ISSN: 0261-4189 (Print) Linking ISSN: 02614189 NLM ISO Abbreviation: EMBO J Subsets: MEDLINE
    • Publication Information:
      Publication: 2024- : [London] : Nature Publishing Group
      Original Publication: Eynsham, Oxford, England : Published for the European Molecular Biology Organization by IRL Press, [c1982-
    • Subject Terms:
      Apoptosis/*physiology ; Bacterial Outer Membrane Proteins/*metabolism ; Calcium/*metabolism ; Cysteine Endopeptidases/*metabolism ; Neisseria gonorrhoeae/*metabolism ; Neisseria gonorrhoeae/*pathogenicity ; Porins/*metabolism; Adenosine Triphosphate/pharmacology ; Amino Acid Chloromethyl Ketones/pharmacology ; Apoptosis/drug effects ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/toxicity ; Calpain/metabolism ; Cell Line ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation/drug effects ; HeLa Cells ; Humans ; Ion Transport/drug effects ; Mutation ; Neisseria gonorrhoeae/genetics ; Porins/genetics ; Porins/toxicity
    • Abstract:
      The porin (PorB) of Neisseria gonorrhoeae is an intriguing bacterial factor owing to its ability to translocate from the outer bacterial membrane into host cell membranes where it modulates the infection process. Here we report on the induction of programmed cell death after prolonged infection of epithelial cells with pathogenic Neisseria species. The underlying mechanism we propose includes translocation of the porin, a transient increase in cytosolic Ca2+ and subsequent activation of the Ca2+ dependent protease calpain as well as proteases of the caspase family. Blocking the porin channel by ATP eliminates the Ca2+ signal and also abolishes its pro-apoptotic function. The neisserial porins share structural and functional homologies with the mitochondrial voltage-dependent anion channels (VDAC). The neisserial porin may be an analogue or precursor of the ancient permeability transition pore, the putative central regulator of apoptosis.
    • References:
      Mol Microbiol. 1992 Nov;6(22):3439-50. (PMID: 1362447)
      Trends Cell Biol. 1996 Nov;6(11):418. (PMID: 15157512)
      Nature. 1992 Jul 9;358(6382):167-9. (PMID: 1614548)
      Cell Death Differ. 1997 Aug;4(6):443-56. (PMID: 16465265)
      EMBO J. 1991 Jun;10(6):1307-15. (PMID: 1673923)
      J Immunol Methods. 1991 Jun 3;139(2):271-9. (PMID: 1710634)
      Res Microbiol. 1991 Nov-Dec;142(9):985-93. (PMID: 1725221)
      Cancer Res. 1991 Sep 1;51(17):4693-700. (PMID: 1873814)
      Biophys J. 1984 Jan;45(1):104-7. (PMID: 19431528)
      Nature. 1990 Nov 22;348(6299):334-6. (PMID: 2250705)
      J Infect Dis. 1989 Dec;160(6):1012-7. (PMID: 2511251)
      J Biol Chem. 1989 Apr 15;264(11):6398-403. (PMID: 2703497)
      Graefes Arch Clin Exp Ophthalmol. 1988;226(4):341-5. (PMID: 3139497)
      Science. 1988 Oct 14;242(4876):256-9. (PMID: 3262923)
      Ann N Y Acad Sci. 1987;503:1-16. (PMID: 3304073)
      Proc R Soc Lond B Biol Sci. 1979 Apr 11;204(1155):267-86. (PMID: 36627)
      Br J Cancer. 1972 Aug;26(4):239-57. (PMID: 4561027)
      Eur J Biochem. 1969 Jun;9(2):245-9. (PMID: 5804498)
      Infect Immun. 1981 Mar;31(3):965-70. (PMID: 6785243)
      J Infect Dis. 1981 Mar;143(3):413-22. (PMID: 6785363)
      Science. 1995 Nov 24;270(5240):1326-31. (PMID: 7481820)
      Neuroscience. 1995 Apr;65(4):1099-108. (PMID: 7617165)
      J Immunol Methods. 1995 Jul 17;184(1):39-51. (PMID: 7622868)
      Cell. 1995 Aug 11;82(3):349-52. (PMID: 7634323)
      Biochim Biophys Acta. 1995 Jul 17;1241(2):139-76. (PMID: 7640294)
      Microb Pathog. 1995 Feb;18(2):81-96. (PMID: 7643745)
      Microb Pathog. 1994 Oct;17(4):203-12. (PMID: 7715420)
      Infect Immun. 1994 Apr;62(4):1304-12. (PMID: 8132337)
      J Cell Physiol. 1994 May;159(2):229-37. (PMID: 8163563)
      Mol Microbiol. 1994 Feb;11(4):619-27. (PMID: 8196540)
      J Exp Med. 1993 Nov 1;178(5):1693-700. (PMID: 8228816)
      Biochem J. 1993 Jan 1;289 ( Pt 1):93-9. (PMID: 8424777)
      J Immunol. 1996 Jan 15;156(2):679-84. (PMID: 8543820)
      Nature. 1996 Mar 7;380(6569):75-9. (PMID: 8598911)
      Cell. 1996 May 3;85(3):391-402. (PMID: 8616894)
      EMBO J. 1996 Aug 1;15(15):3853-60. (PMID: 8670890)
      Mol Gen Genet. 1996 Mar 20;250(5):558-69. (PMID: 8676859)
      Nature. 1996 May 23;381(6580):335-41. (PMID: 8692274)
      Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9833-8. (PMID: 8790417)
      Mol Microbiol. 1996 Apr;20(1):119-26. (PMID: 8861210)
      Science. 1996 Nov 1;274(5288):782-4. (PMID: 8864118)
      Science. 1996 Nov 1;274(5288):787-9. (PMID: 8864120)
      Mol Microbiol. 1996 Sep;21(5):1101-15. (PMID: 8885278)
      Cell. 1996 Nov 1;87(3):565-76. (PMID: 8898208)
      FEBS Lett. 1996 Nov 4;396(2-3):189-95. (PMID: 8914985)
      Biochem J. 1996 Nov 1;319 ( Pt 3):683-90. (PMID: 8920967)
      J Biol Chem. 1996 Dec 6;271(49):31277-82. (PMID: 8940132)
      Science. 1996 Dec 13;274(5294):1859-66. (PMID: 8943190)
      Infect Immun. 1996 Dec;64(12):4900-6. (PMID: 8945524)
      Nat Toxins. 1996;4(5):234-41. (PMID: 8946399)
      Nature. 1997 Jan 23;385(6614):353-7. (PMID: 9002522)
      Science. 1997 Feb 21;275(5303):1132-6. (PMID: 9027315)
      Science. 1997 Feb 21;275(5303):1081-2. (PMID: 9054009)
      EMBO J. 1997 Apr 1;16(7):1695-709. (PMID: 9130714)
      Science. 1997 Jun 6;276(5318):1571-4. (PMID: 9171063)
      Nat Med. 1997 Jun;3(6):614-20. (PMID: 9176486)
      Nature. 1997 Jun 19;387(6635):773-6. (PMID: 9194558)
      J Exp Med. 1997 Jul 21;186(2):247-58. (PMID: 9221754)
      Infect Immun. 1997 Aug;65(8):3391-8. (PMID: 9234803)
      Trends Biochem Sci. 1997 Aug;22(8):299-306. (PMID: 9270303)
      Proc Natl Acad Sci U S A. 1997 Sep 16;94(19):10385-90. (PMID: 9294220)
      Bioessays. 1997 Sep;19(9):827-32. (PMID: 9297974)
      Biochem Biophys Res Commun. 1997 Oct 20;239(2):626-32. (PMID: 9344882)
      Infect Immun. 1997 Nov;65(11):4813-21. (PMID: 9353070)
      Trends Biochem Sci. 1997 Oct;22(10):388-93. (PMID: 9357314)
      Cell. 1997 Nov 14;91(4):443-6. (PMID: 9390553)
      Cell. 1997 Nov 14;91(4):479-89. (PMID: 9390557)
      Cell. 1997 Nov 28;91(5):605-15. (PMID: 9393854)
      EMBO J. 1998 Jan 2;17(1):37-49. (PMID: 9427739)
      EMBO J. 1998 Jan 15;17(2):443-54. (PMID: 9430636)
      J Biol Chem. 1998 Jan 16;273(3):1769-75. (PMID: 9430725)
      J Exp Med. 1998 Sep 7;188(5):941-52. (PMID: 9730895)
      J Exp Med. 1998 Oct 5;188(7):1277-86. (PMID: 9763607)
    • Accession Number:
      0 (Amino Acid Chloromethyl Ketones)
      0 (Bacterial Outer Membrane Proteins)
      0 (Cysteine Proteinase Inhibitors)
      0 (Porins)
      0 (benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone)
      0 (porin protein, Neisseria)
      8L70Q75FXE (Adenosine Triphosphate)
      EC 3.4.22.- (Calpain)
      EC 3.4.22.- (Cysteine Endopeptidases)
      SY7Q814VUP (Calcium)
    • Publication Date:
      Date Created: 19990116 Date Completed: 19990315 Latest Revision: 20181113
    • Publication Date:
      20250114
    • Accession Number:
      PMC1171129
    • Accession Number:
      10.1093/emboj/18.2.339
    • Accession Number:
      9889191