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Virulence-related outer membrane protein family

January 01, 1970

Virulence-related outer membrane proteins, or outer surface proteins (Osp) in some contexts, are expressed in the outer membrane of gram-negative bacteria and are essential to bacterial survival within macrophages and for eukaryotic cell invasion.

Virulence-related OMP
E. coli OmpX, PDB: 1qj8​.
Identifiers
SymbolAil_Lom
PfamPF06316
InterProIPR000758
PROSITEPDOC00582
SCOP21qj9 / SCOPe / SUPFAM
OPM superfamily26
OPM protein1qj8
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ormA:24-171 1q9gA:24-171 1qj8A:24-171

This family consists of several bacterial and phage Ail/Lom-like proteins. The Yersinia enterocolitica Ail protein is a known virulence factor. Proteins in this family are predicted to consist of eight transmembrane beta-sheets and four cell surface-exposed loops. It is thought that Ail directly promotes invasion and loop 2 contains an active site, perhaps a receptor-binding domain. The phage protein Lom is expressed during lysogeny, and encode host-cell envelope proteins. Lom is found in the bacterial outer membrane, and is homologous to virulence proteins of two other enterobacterial genera. It has been suggested that lysogeny may generally have a role in bacterial survival in animal hosts, and perhaps in pathogenesis.

Borrelia burgdorferi (responsible for Lyme disease) outer surface proteins play a role in persistence within ticks (OspA, OspB, OspD), mammalian host transmission (OspC, BBA64), host cell adhesion (OspF, BBK32, DbpA, DbpB), and in evasion of the host immune system (VlsE). OspC trigger innate immune system via signaling through TLR1, TLR2 and TLR6 receptors.[1]

Examples edit

Members of this group include:

  • PagC, required by Salmonella typhimurium for survival in macrophages and for virulence in mice[2]
  • Rck outer membrane protein of the S. typhimurium and S. enteritidis virulence plasmid[3]
  • Ail, a product of the Yersinia enterocolitica chromosome capable of mediating bacterial adherence to and invasion of epithelial cell lines[4]
  • OmpX from Escherichia coli that promotes adhesion to and entry into mammalian cells. It also has a role in the resistance against attack by the human complement system[5]
  • a Bacteriophage lambda outer membrane protein, Lom[6]
  • OspA/B are lipoproteins from Borrelia burgdorferi. OspA and OspB share 53% amino acid identity and likely have a similar antiparallel “free-standing” β sheet protein structure associated with the outer membrane surface via a lipidated NH2-terminal cysteine residue.[7] OspA
  • OspC is a major surface lipoprotein produced by Borrelia burgdorferi when infected ticks feed. OspC is necessary for tick salivary gland invasion.[8] OspC-deficient B. burgdorferi have a markedly reduced capacity (approximately 800-fold less than control spirochetes, OspC expressing) for successful transmission to mice.[9] Its synthesis decreases after transmission to a mammalian host.[10] This protein disappears from the bacterial surface around 2 weeks after infection.[11]

Structure edit

The crystal structure of OmpX from E. coli reveals that OmpX consists of an eight-stranded antiparallel all-next-neighbour beta barrel.[12] The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior. The core of the barrel consists of an extended hydrogen bonding network of highly conserved residues. OmpX thus resembles an inverse micelle. The OmpX structure shows that the membrane-spanning part of the protein is much better conserved than the extracellular loops. Moreover, these loops form a protruding beta sheet, the edge of which presumably binds to external proteins. It is suggested that this type of binding promotes cell adhesion and invasion and helps defend against the complement system. Although OmpX has the same beta-sheet topology as the structurally related outer membrane protein A (OmpA) InterPro: IPR000498, their barrels differ with respect to the shear numbers and internal hydrogen-bonding networks.

OspA from Borrelia burgdorferi is an unusual outer surface protein, it has two globular domains which are connected with a single-layer β-sheet. This protein is highly soluble, contains a large number of Lys and Glu residues. These high entropy residues may disfavor crystal packing.[13]

References edit

  1. ^ Oosting, Marije; Buffen, Kathrin; Meer, Jos W. M. van der; Netea, Mihai G.; Joosten, Leo A. B. (2016-03-03). "Innate immunity networks during infection with Borrelia burgdorferi". Critical Reviews in Microbiology. 42 (2): 233–244. doi:10.3109/1040841X.2014.929563. ISSN 1040-841X. PMID 24963691. S2CID 44840482.
  2. ^ Miller SI (1991). "PhoP/PhoQ: macrophage-specific modulators of Salmonella virulence?". Mol. Microbiol. 5 (9): 2073–2078. doi:10.1111/j.1365-2958.1991.tb02135.x. PMID 1766380. S2CID 40511708.
  3. ^ Cirillo DM, Heffernan EJ, Wu L, Harwood J, Fierer J, Guiney DG (1996). "Identification of a domain in Rck, a product of the Salmonella typhimurium virulence plasmid, required for both serum resistance and cell invasion". Infect. Immun. 64 (6): 2019–2023. doi:10.1128/IAI.64.6.2019-2023.1996. PMC 174031. PMID 8675302.
  4. ^ Miller VL, Bliska JB, Falkow S (1990). "Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product". J. Bacteriol. 172 (2): 1062–1069. doi:10.1128/jb.172.2.1062-1069.1990. PMC 208537. PMID 1688838.
  5. ^ Tommassen J, Stoorvogel J, van Bussel MJ, van de Klundert JA (1991). "Molecular characterization of an Enterobacter cloacae outer membrane protein (OmpX)". J. Bacteriol. 173 (1): 156–160. doi:10.1128/jb.173.1.156-160.1991. PMC 207169. PMID 1987115.
  6. ^ Pulkkinen WS, Miller SI (1991). "A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein". J. Bacteriol. 173 (1): 86–93. doi:10.1128/jb.173.1.86-93.1991. PMC 207160. PMID 1846140.
  7. ^ Templeton, Thomas J. (2004-03-01). "Borrelia Outer Membrane Surface Proteins and Transmission Through the Tick". Journal of Experimental Medicine. 199 (5): 603–606. doi:10.1084/jem.20040033. ISSN 0022-1007. PMC 2213303. PMID 14981110.
  8. ^ Pal, Utpal; Yang, Xiaofeng; Chen, Manchuan; Bockenstedt, Linda K.; Anderson, John F.; Flavell, Richard A.; Norgard, Michael V.; Fikrig, Erol (2004-01-15). "OspC facilitates Borrelia burgdorferi invasion of Ixodes scapularis salivary glands". Journal of Clinical Investigation. 113 (2): 220–230. doi:10.1172/JCI19894. ISSN 0021-9738. PMC 311436. PMID 14722614.
  9. ^ Pal, Utpal; Yang, Xiaofeng; Chen, Manchuan; Bockenstedt, Linda K.; Anderson, John F.; Flavell, Richard A.; Norgard, Michael V.; Fikrig, Erol (2004-01-15). "OspC facilitates Borrelia burgdorferi invasion of Ixodes scapularis salivary glands". Journal of Clinical Investigation. 113 (2): 220–230. doi:10.1172/JCI19894. ISSN 0021-9738. PMC 311436. PMID 14722614.
  10. ^ Tilly, Kit; Krum, Jonathan G.; Bestor, Aaron; Jewett, Mollie W.; Grimm, Dorothee; Bueschel, Dawn; Byram, Rebecca; Dorward, David; VanRaden, Mark J. (2006-06-01). "Borrelia burgdorferi OspC Protein Required Exclusively in a Crucial Early Stage of Mammalian Infection". Infection and Immunity. 74 (6): 3554–3564. doi:10.1128/IAI.01950-05. ISSN 0019-9567. PMC 1479285. PMID 16714588.
  11. ^ Crother, Timothy R.; Champion, Cheryl I.; Whitelegge, Julian P.; Aguilera, Rodrigo; Wu, Xiao-Yang; Blanco, David R.; Miller, James N.; Lovett, Michael A. (2004-09-01). "Temporal Analysis of the Antigenic Composition of Borrelia burgdorferi during Infection in Rabbit Skin". Infection and Immunity. 72 (9): 5063–5072. doi:10.1128/IAI.72.9.5063-5072.2004. ISSN 0019-9567. PMC 517453. PMID 15321999.
  12. ^ Schulz GE, Vogt J (1999). "The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence". Structure. 7 (10): 1301–1309. doi:10.1016/S0969-2126(00)80063-5. PMID 10545325.
  13. ^ Makabe, Koki; Tereshko, Valentina; Gawlak, Grzegorz; Yan, Shude; Koide, Shohei (2006-08-01). "Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering". Protein Science. 15 (8): 1907–1914. doi:10.1110/ps.062246706. ISSN 1469-896X. PMC 2242579. PMID 16823038.

Further reading edit

  • Miller VL, Beer KB, Heusipp G, Young BM, Wachtel MR (September 2001). "Identification of regions of Ail required for the invasion and serum resistance phenotypes". Mol. Microbiol. 41 (5): 1053–62. doi:10.1046/j.1365-2958.2001.02575.x. PMID 11555286. S2CID 5608645.
  • Barondess JJ, Beckwith J (August 1990). "A bacterial virulence determinant encoded by lysogenic coliphage lambda". Nature. 346 (6287): 871–4. Bibcode:1990Natur.346..871B. doi:10.1038/346871a0. PMID 2144037.

January 01, 1970
virulence, related, outer, membrane, protein, family, virulence, related, outer, membrane, proteins, outer, surface, proteins, some, contexts, expressed, outer, membrane, gram, negative, bacteria, essential, bacterial, survival, within, macrophages, eukaryotic. Virulence related outer membrane proteins or outer surface proteins Osp in some contexts are expressed in the outer membrane of gram negative bacteria and are essential to bacterial survival within macrophages and for eukaryotic cell invasion Virulence related OMPE coli OmpX PDB 1qj8 IdentifiersSymbolAil LomPfamPF06316InterProIPR000758PROSITEPDOC00582SCOP21qj9 SCOPe SUPFAMOPM superfamily26OPM protein1qj8Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDB1orm A 24 171 1q9g A 24 171 1qj8 A 24 171 This family consists of several bacterial and phage Ail Lom like proteins The Yersinia enterocolitica Ail protein is a known virulence factor Proteins in this family are predicted to consist of eight transmembrane beta sheets and four cell surface exposed loops It is thought that Ail directly promotes invasion and loop 2 contains an active site perhaps a receptor binding domain The phage protein Lom is expressed during lysogeny and encode host cell envelope proteins Lom is found in the bacterial outer membrane and is homologous to virulence proteins of two other enterobacterial genera It has been suggested that lysogeny may generally have a role in bacterial survival in animal hosts and perhaps in pathogenesis Borrelia burgdorferi responsible for Lyme disease outer surface proteins play a role in persistence within ticks OspA OspB OspD mammalian host transmission OspC BBA64 host cell adhesion OspF BBK32 DbpA DbpB and in evasion of the host immune system VlsE OspC trigger innate immune system via signaling through TLR1 TLR2 and TLR6 receptors 1 Contents 1 Examples 2 Structure 3 References 4 Further readingExamples editMembers of this group include PagC required by Salmonella typhimurium for survival in macrophages and for virulence in mice 2 Rck outer membrane protein of the S typhimurium and S enteritidis virulence plasmid 3 Ail a product of the Yersinia enterocolitica chromosome capable of mediating bacterial adherence to and invasion of epithelial cell lines 4 OmpX from Escherichia coli that promotes adhesion to and entry into mammalian cells It also has a role in the resistance against attack by the human complement system 5 a Bacteriophage lambda outer membrane protein Lom 6 OspA B are lipoproteins from Borrelia burgdorferi OspA and OspB share 53 amino acid identity and likely have a similar antiparallel free standing b sheet protein structure associated with the outer membrane surface via a lipidated NH2 terminal cysteine residue 7 OspA OspC is a major surface lipoprotein produced by Borrelia burgdorferi when infected ticks feed OspC is necessary for tick salivary gland invasion 8 OspC deficient B burgdorferi have a markedly reduced capacity approximately 800 fold less than control spirochetes OspC expressing for successful transmission to mice 9 Its synthesis decreases after transmission to a mammalian host 10 This protein disappears from the bacterial surface around 2 weeks after infection 11 Structure editThe crystal structure of OmpX from E coli reveals that OmpX consists of an eight stranded antiparallel all next neighbour beta barrel 12 The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior The core of the barrel consists of an extended hydrogen bonding network of highly conserved residues OmpX thus resembles an inverse micelle The OmpX structure shows that the membrane spanning part of the protein is much better conserved than the extracellular loops Moreover these loops form a protruding beta sheet the edge of which presumably binds to external proteins It is suggested that this type of binding promotes cell adhesion and invasion and helps defend against the complement system Although OmpX has the same beta sheet topology as the structurally related outer membrane protein A OmpA InterPro IPR000498 their barrels differ with respect to the shear numbers and internal hydrogen bonding networks OspA from Borrelia burgdorferi is an unusual outer surface protein it has two globular domains which are connected with a single layer b sheet This protein is highly soluble contains a large number of Lys and Glu residues These high entropy residues may disfavor crystal packing 13 References edit Oosting Marije Buffen Kathrin Meer Jos W M van der Netea Mihai G Joosten Leo A B 2016 03 03 Innate immunity networks during infection with Borrelia burgdorferi Critical Reviews in Microbiology 42 2 233 244 doi 10 3109 1040841X 2014 929563 ISSN 1040 841X PMID 24963691 S2CID 44840482 Miller SI 1991 PhoP PhoQ macrophage specific modulators of Salmonella virulence Mol Microbiol 5 9 2073 2078 doi 10 1111 j 1365 2958 1991 tb02135 x PMID 1766380 S2CID 40511708 Cirillo DM Heffernan EJ Wu L Harwood J Fierer J Guiney DG 1996 Identification of a domain in Rck a product of the Salmonella typhimurium virulence plasmid required for both serum resistance and cell invasion Infect Immun 64 6 2019 2023 doi 10 1128 IAI 64 6 2019 2023 1996 PMC 174031 PMID 8675302 Miller VL Bliska JB Falkow S 1990 Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product J Bacteriol 172 2 1062 1069 doi 10 1128 jb 172 2 1062 1069 1990 PMC 208537 PMID 1688838 Tommassen J Stoorvogel J van Bussel MJ van de Klundert JA 1991 Molecular characterization of an Enterobacter cloacae outer membrane protein OmpX J Bacteriol 173 1 156 160 doi 10 1128 jb 173 1 156 160 1991 PMC 207169 PMID 1987115 Pulkkinen WS Miller SI 1991 A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein J Bacteriol 173 1 86 93 doi 10 1128 jb 173 1 86 93 1991 PMC 207160 PMID 1846140 Templeton Thomas J 2004 03 01 Borrelia Outer Membrane Surface Proteins and Transmission Through the Tick Journal of Experimental Medicine 199 5 603 606 doi 10 1084 jem 20040033 ISSN 0022 1007 PMC 2213303 PMID 14981110 Pal Utpal Yang Xiaofeng Chen Manchuan Bockenstedt Linda K Anderson John F Flavell Richard A Norgard Michael V Fikrig Erol 2004 01 15 OspC facilitates Borrelia burgdorferi invasion of Ixodes scapularis salivary glands Journal of Clinical Investigation 113 2 220 230 doi 10 1172 JCI19894 ISSN 0021 9738 PMC 311436 PMID 14722614 Pal Utpal Yang Xiaofeng Chen Manchuan Bockenstedt Linda K Anderson John F Flavell Richard A Norgard Michael V Fikrig Erol 2004 01 15 OspC facilitates Borrelia burgdorferi invasion of Ixodes scapularis salivary glands Journal of Clinical Investigation 113 2 220 230 doi 10 1172 JCI19894 ISSN 0021 9738 PMC 311436 PMID 14722614 Tilly Kit Krum Jonathan G Bestor Aaron Jewett Mollie W Grimm Dorothee Bueschel Dawn Byram Rebecca Dorward David VanRaden Mark J 2006 06 01 Borrelia burgdorferi OspC Protein Required Exclusively in a Crucial Early Stage of Mammalian Infection Infection and Immunity 74 6 3554 3564 doi 10 1128 IAI 01950 05 ISSN 0019 9567 PMC 1479285 PMID 16714588 Crother Timothy R Champion Cheryl I Whitelegge Julian P Aguilera Rodrigo Wu Xiao Yang Blanco David R Miller James N Lovett Michael A 2004 09 01 Temporal Analysis of the Antigenic Composition of Borrelia burgdorferi during Infection in Rabbit Skin Infection and Immunity 72 9 5063 5072 doi 10 1128 IAI 72 9 5063 5072 2004 ISSN 0019 9567 PMC 517453 PMID 15321999 Schulz GE Vogt J 1999 The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence Structure 7 10 1301 1309 doi 10 1016 S0969 2126 00 80063 5 PMID 10545325 Makabe Koki Tereshko Valentina Gawlak Grzegorz Yan Shude Koide Shohei 2006 08 01 Atomic resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering Protein Science 15 8 1907 1914 doi 10 1110 ps 062246706 ISSN 1469 896X PMC 2242579 PMID 16823038 Further reading editMiller VL Beer KB Heusipp G Young BM Wachtel MR September 2001 Identification of regions of Ail required for the invasion and serum resistance phenotypes Mol Microbiol 41 5 1053 62 doi 10 1046 j 1365 2958 2001 02575 x PMID 11555286 S2CID 5608645 Barondess JJ Beckwith J August 1990 A bacterial virulence determinant encoded by lysogenic coliphage lambda Nature 346 6287 871 4 Bibcode 1990Natur 346 871B doi 10 1038 346871a0 PMID 2144037 Retrieved from https en wikipedia org w index php title Virulence related outer membrane protein family amp oldid 1150177375, wikipedia, wiki, book, books, library,

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