CoChat
Sign Up
Cited by 251

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Housekeeping enzymes as virulence factors for pathogens

Pancholi, Vijay, Chhatwal, Gursharan S.·2003·International Journal of Medical Microbiology
DOI 10.1078/1438-4221-00283
Open this paper in CoChat — free account

Abstract

Housekeeping enzymes are ubiquitously present in almost all living beings to perform essential metabolic functions for the purpose of survival. These enzymes have been characterized in detail for many years. In recent years, there has been a number of reports indicating that some of these enzymes perform a variety of other functions. In case of many pathogens, certain enzymes play a role to enhance virulence. To perform such a function, enzymes must be located on the surface of pathogens. Although they do not have the typical signal sequence or membrane anchoring mechanisms, they do get secreted and are displayed on the surface, probably by their reassociation. Once on the surface, these enzymes interact with host components, such as fibronectin and plasminogen, or interact directly with the host cells, to trigger signal transduction and thereby enable the pathogens to colonize, persist and invade the host tissue. Therefore, certain housekeeping enzymes may act as putative virulence factors and targets for the development of new strategies to control the infection by using agents that can block their secretion and/or reassociation.

Overview

Integrity signals

Registry

Crossref · 10.1078/1438-4221-00283

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 2 references

Research works printed but not linked: 74

  1. Alderete, 2001, Enzymes on microbial pathogens and Trichomonas vaginalis: molecular mimicry and functional diversity, Cell. Microbiol., 3, 359, 10.1046/j.1462-5822.2001.00126.x · DOI
  2. Allen, 1995, Case study: a new infection-triggered, autoimmune subtype of pediatric OCD and Tourette's syndrome, J. Am. Acad. Child Adolesc. Psychiatry, 34, 307, 10.1097/00004583-199503000-00015 · DOI
  3. Alloush, 1997, 3-Phosphoglycerate kinase: a glycolytic enzyme protein present in the cell wall of Candida albicans, Microbiology, 143, 321, 10.1099/00221287-143-2-321 · DOI
  4. Angiolella, 1996, Identification of a glucanassociated enolase as a main cell wall protein of Candida albicans and an indirect target of lipopeptide antimycotics, J. Infect. Dis., 173, 684, 10.1093/infdis/173.3.684 · DOI
  5. Baldo, 1988, Inhalant allergies to fungi: reactions to bakers' yeast (Saccharomyces cerevisiae) and identification of bakers' yeast enolase as an important allergen, Int. Arch. Allergy Appl. Immunol, 86, 201, 10.1159/000234572 · DOI
  6. Baseman, 1997, Mycoplasmas: sophisticated, reemerging, and burdened by their notoriety, Emerg. Infect. Dis., 3, 21, 10.3201/eid0301.970103 · DOI
  7. Berge, 1993, PAM, a novel plasminogen-binding protein from Streptococcus pyogenenes, J. Biol. Chem., 268, 25417, 10.1016/S0021-9258(19)74408-1 · DOI
  8. Bergmann, 2001, Alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface, Mol. Microbiol., 40, 1273, 10.1046/j.1365-2958.2001.02448.x · DOI
  9. Bergmann, 2003, Identification of a novel plasmin(ogen)-binding motif in surface-displayed alpha-enolase of Streptococcus pneumoniae, Mol Microbiol., 49, 411, 10.1046/j.1365-2958.2003.03557.x · DOI
  10. Bermudez, 1996, Epidermal growth factor-binding protein in Mycobacterium avium and Mycobacterium tuberculosis: a possible role in the mechanism of infection, Infect. Immun., 64, 2917, 10.1128/iai.64.8.2917-2922.1996 · DOI
  11. Boyle, 1997, Plasminogen activation by invasive human pathogens, Thromb. Haemost., 77, 1, 10.1055/s-0038-1655727 · DOI
  12. Brewer, 1997, Current perspectives on the mechanism of catalysis by the enzyme enolase, Adv. Biophys. Chem., 6, 111
  13. Broeseker, 1988, Characterization of the interaction of human plasmin with its specific receptor on a group A streptococcus, Microb. Pathog., 5, 19, 10.1016/0882-4010(88)90077-0 · DOI
  14. Camara, 1994, A neuraminidase from Streptococcus pneumoniae has the features of a surface protein, Infect. Immun., 62, 3688, 10.1128/iai.62.9.3688-3695.1994 · DOI
  15. Cash, 1999, A proteomic analysis of erythromycin resistance in Streptococcus pneumoniae, Electrophoresis, 20, 2259, 10.1002/(SICI)1522-2683(19990801)20:11<2259::AID-ELPS2259>3.0.CO;2-F · DOI
  16. Clewell, 1995, Unconstrained bacterial promiscuity: the Tn916-Tn1545 family of conjugative transposons, Trends Microbiol., 3, 229, 10.1016/S0966-842X(00)88930-1 · DOI
  17. Dallo, 2002, Elongation factor Tu and E1 alpha subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae, Mol. Microbiol., 46, 1041, 10.1046/j.1365-2958.2002.03207.x · DOI
  18. Degado, 2001, The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins, Microbiology, 147, 411, 10.1099/00221287-147-2-411 · DOI
  19. D'Costa, 2000, Analysis of expression of a cytosolic enzyme on the surface of Streptococcus pyogenes, Biophys. Res Commun., 278, 826, 10.1006/bbrc.2000.3884 · DOI
  20. Engbring, 1998, Three genes encode distinct AP33 proteins involved in Trichomonas vaginalis cytoadherence, Mol. Microbiol., 28, 305, 10.1046/j.1365-2958.1998.00784.x · DOI
  21. Engbring, 1996, Trichomonas vaginalis adhesin proteins display molecular mimicry to metabolic enzymes, Adv. Exp. Med. Biol., 408, 207, 10.1007/978-1-4613-0415-9_25 · DOI
  22. Espinosa-Urgel, 1998, Escherichia coli expressed preferentially in an aquatic environment, Mol. Microbiol., 28, 325, 10.1046/j.1365-2958.1998.00796.x · DOI
  23. Facinelli, 2001, Association between erythromycin resistance and ability to enter human respiratory cells in group A streptococci, Lancet, 358, 30, 10.1016/S0140-6736(00)05253-3 · DOI
  24. Fernandes, 1992, A protein homologous to glyceraldehyde-3-phosphate dehydrogenase is induced in the cell wall of a flocculent Kluyveromyces marxianus, Biochim. Biophys. Acta, 1159, 67, 10.1016/0167-4838(92)90076-P · DOI
  25. Fletcher, 2001, Analysis of the effect of changing environmental conditions on the expression patterns of exported surface-associated proteins of the oral pathogen Actinobacillus actinomycetemcomitans, Microb. Pathog., 30, 359, 10.1006/mpat.2000.0439 · DOI
  26. Fontan, 2000, Antibodies to streptococcal surface enolase react with human alpha-enolase: Implications in poststreptococcal sequelae, J. Infect. Dis., 182, 1712, 10.1086/317604 · DOI
  27. Fox, 2001, Plasminogen-binding activity of enolase in the opportunistic pathogen Pneumocystis carinii, Med. Mycol., 39, 495, 10.1080/mmy.39.6.495.507 · DOI
  28. Gil-Navarro, 1997, The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen, J. Bacteriol, 179, 4992, 10.1128/jb.179.16.4992-4999.1997 · DOI
  29. Goudot-Crozel, 1989, The major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde-3P-dehydrogenase, J. Exp. Med., 170, 2065, 10.1084/jem.170.6.2065 · DOI
  30. Gozalbo, 1998, The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein, Infect. Immun., 66, 2052, 10.1128/IAI.66.5.2052-2059.1998 · DOI
  31. Grifantini, 2002, Gene expression profile in Neisseria meningitidis and Neisseria lactamica upon host-cell contact: from basic research to vaccine development, Ann. N.Y. Acad. Sci., 975, 202, 10.1111/j.1749-6632.2002.tb05953.x · DOI
  32. Guzman, 1990, Role of neuraminidase-dependent adherence in Bacteroides fragilis attachment to human epithelial cells, FEMS Microbiol. Lett., 59, 187, 10.1111/j.1574-6968.1990.tb03820.x · DOI
  33. Hara, 2000, Cell surface-associated enolase in Actinobacillus actinomycetemcomitans, Microbiol. Immunol., 44, 349, 10.1111/j.1348-0421.2000.tb02505.x · DOI
  34. Ishiguro, 1992, Identification of Candida albicans antigens reactive with immunoglobulin E antibody of human sera, Infect. Immun., 60, 1550, 10.1128/iai.60.4.1550-1557.1992 · DOI
  35. Jolodar, 2003, Molecular cloning of an alpha-enolase from the human filarial parasite Onchocerca volvulus that binds human plasminogen, Biochim. Biophys. Acta, 1627, 111, 10.1016/S0167-4781(03)00083-6 · DOI · Paper page
  36. Jones, 2000, Reactivity of rheumatic fever and scarlet fever patients' sera with group A streptococcal M protein, cardiac myosin, and cardiac tropomyosin: a retrospective study, Infect. Immun., 68, 7132, 10.1128/IAI.68.12.7132-7136.2000 · DOI
  37. Kaufmann, 1992, Purification, characterization and inhibition by fluoride of enolase from Streptococcus mutans DSM 320523, Caries Res., 26, 110, 10.1159/000261494 · DOI
  38. Kenny, 1995, Protein secretion by enteropathogenic Escherichia coli is essential for transducting signals to epithelial cells, Proc. Natl. Acad. Sci. USA, 92, 7791, 10.1073/pnas.92.17.7991 · DOI
  39. Konings, 1983, Energy transduction and solute transport in streptococci, Antonie van Leeuwenhoek, 49, 247, 10.1007/BF00399501 · DOI
  40. Lee, 1995, Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene product, Mol. Biochem. Parasitol., 71, 221, 10.1016/0166-6851(95)91598-O · DOI
  41. Lee, 1995, Immune response to Schistosoma mansoni phosphoglycerate kinase during natural and experimental infection: Identification of a schistosome-specific B-cell epitope, Infect. Immun., 63, 4307, 10.1128/iai.63.11.4307-4311.1995 · DOI
  42. Lei, 2000, Identification and immunogenicity of group A Streptococcus culture supernatant proteins, Infect. Immun., 68, 6807, 10.1128/IAI.68.12.6807-6818.2000 · DOI
  43. Lottenberg, 1992, Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor, J. Bacteriol., 174, 5204, 10.1128/jb.174.16.5204-5210.1992 · DOI
  44. Lottenberg, 1994, Capturing host plasmin(ogen): a common mechanism for invasive pathogens?, Trends Microbiol., 2, 20, 10.1016/0966-842X(94)90340-9 · DOI
  45. Miles, 1991, Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor, Biochemistry, 30, 1682, 10.1021/bi00220a034 · DOI · Paper page
  46. Modun, 2000, The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions, Trends Microbiol., 8, 231, 10.1016/S0966-842X(00)01728-5 · DOI
  47. Modun, 1999, The staphylococcal transferrinbinding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase, Infect. Immun., 67, 1086, 10.1128/IAI.67.3.1086-1092.1999 · DOI · Paper page
  48. Morgan, 1979, Studies on the mechanism of iron release from transferrin, Biochim. Biophys. Acta, 580, 312, 10.1016/0005-2795(79)90144-2 · DOI
  49. Moss, 1988, ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins, Adv. Enzymol., 61, 303
  50. Nakajima, 1994, Plasminogen binds specifically to alpha-enolase on rat neuronal plasma membrane, J. Neurochem., 63, 2048, 10.1046/j.1471-4159.1994.63062048.x · DOI
  51. Nelson, 2001, pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: Purification, characterization, and cloning of the gene encoding this enzyme, J. Dent. Res., 80, 371, 10.1177/00220345010800011301 · DOI
  52. Pancholi, 2001, Multifunctional alpha-enolase: its role in diseases, Cell. Mol. Life Sci., 58, 902, 10.1007/PL00000910 · DOI
  53. Pancholi, 1992, A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate dehydrogenase with multiple binding activity, J. Exp. Med., 176, 415, 10.1084/jem.176.2.415 · DOI
  54. Pancholi, 1993, Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme, Proc. Natl. Acad. Sci. USA, 90, 8154, 10.1073/pnas.90.17.8154 · DOI
  55. Pancholi, 1997, Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase(SDH): Signal transduction between streptococci and pharyngeal cells, J. Exp. Med., 186, 1633, 10.1084/jem.186.10.1633 · DOI · Paper page
  56. Pancholi, 1998, Alpha-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci, J. Biol. Chem., 273, 14503, 10.1074/jbc.273.23.14503 · DOI
  57. Pancholi, 2003, Plasminogen-mediated group A streptococcal adherence to and pericellular invasion of human pharyngeal cells, Microb. Pathog, 35, 293, 10.1016/j.micpath.2003.08.004 · DOI
  58. Plow, 1995, The cell biology of the plasminogen system, FASEB. J., 9, 939, 10.1096/fasebj.9.10.7615163 · DOI
  59. Redlitz, 1995, The role of an enolase-related molecule in plasminogen binding to cells, Eur. J. Biochem., 227, 407, 10.1111/j.1432-1033.1995.tb20403.x · DOI
  60. Roberts, 1980, Phosphoenolpyruvate-dependent glucose phosphotransferase activity in Streptococcus mitis ATCC 903, Scand. J. Dent. Res., 88, 316
  61. Sha, 2003, Differential expression of the enolase gene under in vivo versus in vitro growth conditions of Aeromonas hydrophila, Microb. Pathog., 34, 195, 10.1016/S0882-4010(03)00028-7 · DOI
  62. Shoemaker, 1992, cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase, Proc. Natl. Acad. Sci. USA, 89, 1842, 10.1073/pnas.89.5.1842 · DOI
  63. Sirover, 1999, New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase, Biochim. Biophys. Acta, 1432, 159, 10.1016/S0167-4838(99)00119-3 · DOI
  64. Smalheiser, 1996, Proteins in unexpected locations, Mol. Biol. Cell, 7, 1003, 10.1091/mbc.7.7.1003 · DOI
  65. Sundstrom, 1992, Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme, J. Bacteriol., 174, 6789, 10.1128/jb.174.21.6789-6799.1992 · DOI
  66. Sutcliffe, 1996, Streptococcus pneumoniae and Streptococcus pyogenes resistant to macrolides but sensitive to clindamycin: a common resistance pattern mediated by an efflux system, Antimicrob. Agents Chemother, 40, 1817, 10.1128/AAC.40.8.1817 · DOI
  67. Swoboda, 1993, Glycolytic enzymes of Candida albicans are nonubiquitous immunogens during candidiasis, Infect. Immun., 61, 4263, 10.1128/iai.61.10.4263-4271.1993 · DOI
  68. Taylor, 2002, Transferrin binding in Staphylococcus aureus: involvement of a cell wallanchored protein, Mol. Microbiol., 43, 1603, 10.1046/j.1365-2958.2002.02850.x · DOI
  69. Vacca-Smith, 1994, Glucosyltransferase mediates adhesion of Streptococcus gordonii to human endothelial cells in vitro, Infect. Immun., 62, 2187, 10.1128/iai.62.6.2187-2194.1994 · DOI
  70. Wistow, 1987, Recruitment of enzymes as lens structural proteins, Science, 236, 1554, 10.1126/science.3589669 · DOI
  71. Wistow, 1988, Taucrystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein, J. Cell Biol., 107, 2729, 10.1083/jcb.107.6.2729 · DOI
  72. Yamakami, 2000, The potential role for nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis, Methods, 21, 185, 10.1006/meth.2000.0990 · DOI
  73. Yang, 1994, Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifuctional adhE gene product of Escherichia coli, Mol. Biochem. Parasitol., 64, 253, 10.1016/0166-6851(93)00020-A · DOI
  74. Yeung, 1993, Complete nucleotide sequence of the Actinomyces viscosus T14V sialidase gene: presence of a conserved repeating sequence among strains of Actinomyces spp, Infect. Immun., 61, 109, 10.1128/iai.61.1.109-116.1993 · DOI

Cited by

Sorted by citations

See all 251

Metadata

Authors
Pancholi, V., & Chhatwal, G. S.
Venue
International Journal of Medical Microbiology
Publisher
Elsevier BV
Published
2003
Volume
293
Issue
6
Pages
391-401
ISSN
1438-4221
DOI
10.1078/1438-4221-00283
Cited by
251
References
2
Language
en
Licence
Funders
  • National Institutes of Health (AI-42827)
  • American Heart Association (EI-9940228N)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Housekeeping enzymes as virulence factors for pathogens. https://app.cochat.ai/papers/10.1078/1438-4221-00283
The paper
Pancholi, V., & Chhatwal, G. S. (2003). Housekeeping enzymes as virulence factors for pathogens. International Journal of Medical Microbiology. https://doi.org/10.1078/1438-4221-00283