Streptococcus pneumoniae hyaluronate lyase: An overview

Current Science

Volumn 86, Issue 2, 2004, Pages 285-295

  Akhtar, Md Sohail ^a   Bhakuni, Vinod ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); POSIBACTERIA; STREPTOCOCCUS; STREPTOCOCCUS PNEUMONIAE;

EID: 4444290679     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (114)

1. Novak, R., Henriques, B., Charpentier, E., Normark, S. and Tuomance, E., Emergence of vancomycin tolerance in Streptococcus pneumoniae. Nature, 1999, 399, 590-593.
2. Boulnois, G. J., Pneumococcal proteins and the pathogenesis of disease caused by Streptococcus pneumoniae. J. Gen. Microbiol., 1992, 138, 249-259.
3. Mufson, M. A., Principle and Practice of Infectious Diseases, Churchill Livingstone, Inc., New York, 1990, pp. 1539-1550.
4. Gray, B. M., Converse III, G. M. and Dillon Jr., H. C., Epidemiological studies of Streptococcus pneumoniae in infants: acquisition, carriage, and infection during the first 24 months of life. J. Infect. Dis., 1980, 142, 923-933.
5. Johnston, Jr. R. B., Pathogenesis of pneumococcal pneumoniae. Rev. Infect. Dis., 1991, 13, S509-S517.
6. Musher, D. M., Infections caused by Streptococcus pneumoniae disical spectrum, pathogenesis, immunity, and treatment. Clin. Infect. Dis., 1991, 1, 801-807.
7. Lancet, Acute respiratory infections in under fives: 15 million deaths a year. Lancet, 1985, II, 699-701.
8. Robinson, K. A. et al., Epidemiology of invasive Streptococcus pneumoniae infection in the United States: 1995-1998. 2001, JAMA, 285, 1729-1735.
9. Baquero, F., Martinez-Beltran, J. and Loza, E., A review of antibiotic resistance patterns of Streptococcus pneumoniae in Europe. J. Antimicrob. Chemother., 1991, 28, 31-38.
10. Pelton, S. I., Acute otitis media in the era of effective pneumococcal vaccine: Will new pathogen emerge. Vaccine, 2000, 19, S96-S99.
11. Mbelle, N. et al., Immunogenicity and impact on nasopharyngeal carriage of a nonavalent pneumococcal conjugate vaccine. J. Infect. Dis., 1999, 180, 1171-1176.
12. Putnam, S. D., Gray, G. C., Biedenbach, D. J. and Jones, R. N., Pharyngeal colonization prevalence rates for Streptococcus pyogenes and Streptococcus pneumoniae in a respiratory chemoprophylaxis intervention study using azithromycin. Clin. Microbiol. Infect., 2000, 6, 2-10.
13. Fraser, J. R. E. and Laurent, T. C., Ciba Found. Symp., 1989, 143, 41-49.
14. Laurent, T. C. and Fraser, J. R. E., Hyaluronan. FASEB, 1992, 6, 2397-2404.
15. Rademacher, T. W., Parekh, R. B. and Dwek, R. A., Glycobiology. Annu. Rev. Biochem., 1988, 57, 785-838.
16. Paulson, J. C., Glycoproteins: What are the sugar chains for? Trends Biochem. Sci., 1989, 14, 272-276.
17. Esko, J. D., Genetic analysis of proteoglycan structure, function and metabolism. Curr. Opin. Cell Biol., 1991, 3, 805-816.
18. Hart, G. W., Glycosylation. Curr. Opin. Cell Biol., 4, 1017-1023.
19. Kobata, A., Structure and function of the sugar chains of glycoproteins. Eur. J Biochem., 1992, 209, 483-501.
20. Lis, H and Sharon, N., Protein glycosylation - structural and functional aspect. Eur. J. Biochem., 1993, 218, 1-27.
21. Varki, A., Biological roles of oligosaccharides: All of the theories are correct. Glycobiology, 1993, 3, 97-130.
22. Varki, A. and Marth, J., Oligosaccharides in vertebrate development. Semin. Dev. Biol., 1995, 6, 127-138.
23. Ghamberg, C. G. and Tolvanen, M., Why mammalian cell surface proteins are glycoproteins. Trends Biochem. Sci., 1996, 21, 308-311.
24. Turley, E. A. and Auersperg, N., A hyaluronate binding protein transiently codistributes with p21k-ras in cultured cell lines. Exp. Cell. Res., 1989, 182, 340-348.
25. Gagneux, P. and Varki, A., Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology, 1999, 9, 747-755.
26. 13C NMR study. Proc. Natl. Acad. Sci. USA, 1999, 96, 4850-4855.
27. Lindahl, U. and Hook, M., Glycosaminoglycans and their binding to biological macromolecules. Annu. Rev. Biochem., 1978, 47, 385-417.
28. Delpech, B., Girard, N., Bertrand, P., Courel, M-N. and Delpech, A., Hyaluronan, fundamental principles and applications in cancer. J. Intern. Med., 1997, 242, 41-48.
29. Laurent, T. C., Chemistry and Molecular Biology of the Intercellular Matrix, Academic Press, London, 1997, pp. 703-732.
30. Hynes, W. L. and Ferreti, J., Sequence analysis and expression E. coli of the hyaluronidase gene of Streptococcus pyogenes bacteriophage H4489A. J. Infect. Immunol., 1989, 57, 533-539.
31. Comper, W. D. and Laurent, T. C., Physiological function of connective tissue polysaccharides. Physiol. Rev., 1978, 58, 255-308.
32. Menzel, E. J. and Farr, C., Hyaluronidase and its substrate hyaluronan: Biochemistry, biological activities and therapeutic uses. Cancer Lett., 1998, 131, 3-11.
33. Drickamer, K. and Taylor, M. E., Evolving views of protein glycosylation. Trends Biochem. Sci., 1998, 23, 321-324.
34. Turley, E. A., Hyaluronic acid stimulates protein kinase activity in intact cells and in an isolated protein complex. J. Biol. Chem., 1989, 264, 8951-8955.
35. Yang, B., Yang, B. L., Savani, R. C. and Turley, E. A., Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. EMBO J., 1994, 13, 288-298.
36. Austen, L., Nance, D. M. and Turley, E. A., Molecular crossing of a novel hyaluronan receptor that mediates tumour cell motility. J. Cell Biol., 1992, 117, 1343-1350.
37. Underhill, C. B. and Toole, B. P., Receptors for hyaluronate on the surface of parent and virus transformed cell lines. Binding and aggregation studies. Exp. Cell Res., 1981, 131, 419-423.
38. Stamenkovic, I., Aruffo, A., Amiot, M. and Seed, B., The hematopoietic and epithelial forms of CD44 are distinct polypeptides with different adhesion potentials for hyaluronate- bearing cells. EMBO J., 1991, 10, 343-348.
39. Thomas, L., Byers, H. R., Vink, J. and Stamenkovic, I., CD44H regulates tumour cell migration on hyaluronate-coated substrate. J. Cell Biol., 1992, 118, 971-978.
40. Cundell, D. R., Pearce, B. J., Sandros, J., Naughton, A. M. and Masure, H. R., Peptide permease from Streptococcus pneumoniae affect adherence to eukaryotic cells. Infect. Immunol., 1995, 63, 2493-2498.
41. Cundell, D. R., Gerard, N. P., Gerard, C., Idanpaan-Heikkila, I. and Toumanen, E., Streptococcus pneumoniae anchor to human cells by the receptor for platelet-activating factor. Nature, 1995, 377, 435-438.
42. Jedrzejas, M. J., Pneumococcal virulence factors: Structure and function. Microbiol. Mol. Biol. Rev., 2001, 65, 187-207.
43. Duran-Raynals, F., Studies on a certain spreading factor existing in bacteria and its significance for bacterial invasiveness. J. Exp. Med., 1933, 58, 161-181.
44. Houck, J. C. and Chang, C. M., Permeability factor contaminating hyaluronidase preparations. Inflammation, 1979, 3, 447-451.
45. Meyer, K. and Palmer, J. W., The polysaccharide of the vitreous humour. J. Biol. Chem., 1934, 107, 629-634.
46. Canard, B., Garnier, T., Saint-Joanis, B. and Cole, S. T., Molecular genetic analysis of the nagH gene encoding a hyaluronidase from Clostridium perfringens. Mol. Gen. Genet., 1994, 243, 215-224.
47. Hynes, W. L. and Ferreti, J. J., Assays for hyaluronidase activity. Methods Enzymol., 1994, 235, 606-616.
48. Meyer, K., The Enzyme, Academic Press, New York, 1971, 3rd edn, pp. 307-320.
49. Poh, C. H., Yuen, R., Chung, M. C. and Khoo, H. E., Purification and partial characterization of hyaluronidase from stonefish (Synanceja horrida) venom. Comp. Biochem. Physiol. B, 1992, 101, 159-163.
50. Tu, A. T. and Hendon, R. R., Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor. Comp. Biochem. Physiol. B, 1983, 76, 377-383.
51. Primakoff, P., Lathrop, W., Woolman, L., Cowan, A. and Myles, D. G., Fully effective contraception in male and female guinea pigs immunized with the sperm protein PH-20. Nature, 1988, 335, 543-546.
52. Genachl, M. and Kreil, G., Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proc. Natl. Acad. Sci. USA, 1993, 90, 3569-3573.
53. Frost, G. I., Csoka, T. B., Wong, T. and Stern, R., Purification cloning, and expression of human plasma hyaluronidase. Biochem. Biophys. Res. Commun., 1997, 236, 10-15.
54. Csoka, T. B., Frost, G. I., Wong, T. and Stern, R., Purification and microsequencing of hyaluronidase isozymes from human urine. FEBS Lett., 1997, 417, 307-310.
55. Highsmith, S., Garvin, J. H. and Chipman, D. M., Mechanism of action of bovine testicular hyaluronidase, mapping of the active site. J. Biol. Chem., 1975, 18, 7473-7480.
56. Cramer, J. A., Bailey, L. C., Bailey, C. A. and Miller, R. T., Kinetic and mechanistic studies with bovine testicular hyaluronidase. Biochim. Biophys. Acta, 1994, 1200, 315-321.
57. Laurent, T. C., Ciba Found. Symp., 1989, 143, 1-298.
58. Takagaki, K. et al., Characterization of hydrolysis and transglycosylation by testicular hyaluronidases using ion-spray mass spectroscopy. Biochemistry, 1994, 33, 6503-6507.
59. Hotez, P., Cappello, M., Hawdon, J., Beckers, C. and Sakanari, J., Hyaluronidases of the gastrointestinal invasive nematodes Ancylostoma canium and Anisakis simplex: Possible functions in the pathogenesis of human zoonoses. J. Infect. Dis., 1994, 170, 918-926.
60. Berry, A. M., Lock, R. A., Thomas, S. M., Rajan, D. P., Hansman, D. and Paton, J. C., Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli. Infect. Immunol., 1994, 62, 1101-1108.
61. Lin, B., Hollingshead, S. K., Coligan, J. E., Egan, M. L., Baker, J. R. and Pritchard, D. G., Cloning and expression of the gene for group B streptococcus hyaluronate lyase. J. Biol. Chem., 1994, 269, 30113-30116.
62. Kreil, G., Hyaluronidase - a group of neglected enzyme. Protein Sci., 1995, 4, 1666-1669.
63. Kelly, S. J., Taylor, K. B., Li, S. and Jedrzejas, M. J., Kinetic properties of Streptococcus pneumoniae hyaluronate lyase. Glycobiology, 2001, 11, 297-304.
64. 13C NMR study Proc. Natl. Acad. Sci. USA, 1999, 96, 4850-4855.
65. Plass, A. H. K., Wong-Palms, S., Roughley, P. J., Midura, R. J. and Hascall, V. C., Chemical and immunological assay of the nonreducing terminal residues of chondroitin sulphate from human aggrecan C. J. Biol. Chem., 1997, 272, 20603-20610.
66. Pritchard, D. G., Trent, J. O., Zhang, P., Egan, M. L. and Baker, J. R., Characterization of the active site of group B Streptococcus hyaluronate lyase. Proteins, 2000, 40, 126-134.
67. Humphrey, J. H., Hyaluronidase production by pneumococci. J. Pathol., 1948, 55, 273-275.
68. Pritchard, D. J. and Lin, B., Group B Streptococcus neuraminidase is actually a hyaluronidase. Infect. Immunol., 1993, 61, 3234-3239.
69. Jedrzejas, M. J., Structural and functional comparison of polysaccharide-degrading enzyme. Crit. Rev. Biochem. Mol. Biol., 2000, 35, 221-251.
70. Busse, W., Pathogenesis and sequelae of respiratory infections. Rev. Infect. Dis., 1991, 13, S477-S485.
71. Ponnuraj, K. and Jedrzejas, M. J., Hyaluronan binding and degradation: A complex structure of Streptococcus pneumoniae hyaluronate lyase with hyaluronan substrate. J. Mol. Biol., 2000, 299, 885-895.
72. Li, S., Kelly, S. J., Lamani, E., Ferraroni, M. and Jedrzejas, M. J., Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. EMBO J., 2000, 19, 1228-1240.
73. Hynes, W. L. and Hancock, L., Analysis of a second bacteriophage hyaluronidase gene from Streptococcus pyogenes: Evidence for a third hyaluronidase involved in extracellular enzymatic activity. Infect. Immunol., 1995, 63, 3015-3020.
74. Steiner, B. and Cruce, D., A zynographic assay for detection of hyaluronidase activity on polyacrylamide gels and its application to enzymatic activity found in bacteria. Anal. Biochem., 1992, 200, 405-410.
75. Jedrzejas, M. J., Mewbourne, R. B., Chantalat, L. and McPherson, D., Expression and purification of Streptococcus pneumoniae hyaluronate lyase from Escherichia coli. Protein Express. Purif., 1998, 13, 83-89.
76. Schneewind, O., Fowler, A. and Faull, K. F., Structure of the cell wall anchor of surface proteins in Staphylococcus aureas. Science, 1995, 268, 103-106.
77. Fischetti, V. A., Pancholi, V. and Schneewind, O., Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram-positive cocci. Mol. Microbiol., 1990, 4, 1603-1605.
78. Pritchard, B. J., Lin, B., Willingham, T. R. and Baker, J. R., Characterization of the group B streptococcus hyaluronate lyase. Arch. Biochem. Biophys., 1994, 315, 431-437.
79. Jedrzejas, M. J., Chantalat, L. and Mewbourne, R. B., Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase. J. Struct. Biol., 1998, 121, 73-75.
80. Li, S. and Jedrzejas, M. J., Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase. J. Biol. Chem., 2001, 276, 41407-41416.
81. Fethiere, J., Eggimann, B. and Cygler, M., Crystal structure of chondroitin AC lyase, a representative of a family of glucosaminoglycan degrading enzyme. J. Mol. Biol., 1999, 288, 635-647.
82. Yoon, H. J., Mikami, B., Hashimoto, W. and Murata, K., Crystal structure of alginate lyase AI-III from Sphingomonas species A1 at 1.78 Å resolution. J. Mol. Biol., 1999, 290, 505-514.
83. Jedrzejas, M. J., Mello, L. V., de Groot, B. L. and Li, S., Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. J. Biol. Chem., 2002, 277, 28287-28297.
84. Aleshin, A., Gloubev, A., Firsov, L. M. and Honzatko, R. B., Crystal structure of glucoamylase from Aspergillus awamorivar. X100 to 2.2 Å resolution. J. Biol. Chem., 1998, 267, 19291-19298.
85. Alzair, P. M., Souchon, H. and Dominguez, R., The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum. Structure, 1996, 4, 265-275.
86. Juy, M., Amit, A. G., Alzari, P. M., Poljak, R. J., Claeyssens, M., Beguin, P. and Aubert, J. P., Three dimensional structure of a thermostable bacterial cellulase. Nature, 1992, 357, 89-91.
87. Sakon, J., Irwin, D., Wilson, D. B. and Karplus, P. A., Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nature Struct. Biol., 1997, 4, 810-818.
88. McCarter, J. D. and Withers, S. G., Mechanism of enzymatic glycoside hydrolysis. Curr. Opin. Struct. Biol., 1994, 4, 885-892.
89. Davies, G. and Henrissat, B., Structures and mechanisms of glycosyl hydrolases. Structure, 1995, 3, 853-859.
90. Chauvaux, S., Souchon, H., Alzari, P. M., Chariot, P. and Beguin, P., Structural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase cell. J. Biol. Chem., 1995, 270, 9757-9762.
91. Nukui, M., Tayler, K. B., McPherson, D. T., Shigenaga, M. K. and Jedrzejas, M. J., The function of hydrophobic residues in the catalytic cleft of Streptococcus pneumoniae hyaluronate lyase. J. Biol. Chem., 2003, 278, 3079-3088.
92. Butler, J. C., Hofmann, J., Cetron, M. S., Elliott, J. A., Facklam, R. R. and Breiman, R. F., The continued emergence of drug resistant Streptococcus pneumoniae in the United States: An update from the centers for disease control and prevention's pneumococacal sentinel surveillance system. J. Infect. Dis., 1996, 174, 986-993.
93. Butler, J. C., Shapiro, E. D. and Carlone, G. M., Pneumococcal vaccines: history, current status, and future directions. Am. J. Med., 1999, 107, 69S-76S.
94. Camara, M., Boulnis, G. J., Andrew, P. W. and Mitchel, T., A neuraminidase from Streptococcus pneumoniae has the features of a surface protein. J. Infect. Immunol., 1994, 62, 3688-3695.
95. Hofmann, J., Cetron, M. S. and Farley, M. M., The prevalence of drug-resistant Streptococcus pneumoniae in Atlanta. J. Med., 1995, 333, 481-486.
96. Berry, A. M. and Paton, J. C., Additive attenuation of virulence of Streptococcus pneumoniae by mutation of the genes encoding pneumolysin and other putative pneumococcal virulence proteins. Infect. Immunol., 2000, 68, 133-140.
97. Feldman, C., Munro, N. C. and Jeffery, P. K., Pneumolysin induces the salient histologic features of pneumococcal infection in the rat lung in vivo. Am. J. Respir. Cell. Mol. Biol., 1992, 5, 416-423.
98. Lock, R. A., Paton, J. C. and Hansman, D., Purification and immunological characterization of neuraminidase produced by Streptococcus pneumoniae. Microb. Pathog., 1988, 5, 461-467.
99. Rosenow, C., Ryan, P., Weiser, J. N., Johnson, S., Fontan, P., Ortqvist, A. and Masure, H. R., Contribution of novel choline-binding protein to adherence, colonization and immunogenicity of Streptococcus pneumoniae. Mol. Microbiol., 1997, 25, 819-829.
100. Sampson, J. S., O'Connor, S. P., Stinson, A. R., Tharpe, J. A. and Russel, H., Cloning and nucleotide sequence analysis of psaA, the Streptococcus pneumoniae gene encoding a 37-kiloDalton protein homologous to previously reported Streptococcus sp. adhesin. Infect. Immunol., 1994, 62, 319-324.
101. McDaniel, L. S., Sheffield, J. S., DeLucchi, P. and Briles, D. E., PspA a surface protein of Streptococcus pneumoniae is capable of eliciting protection against pneumococci of more than one capsular type. Infect. Immunol., 1991, 59, 222-228.
102. Loeffler, J. M., Nelson, D. and Fischetti, V., Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science, 2001, 294, 2170-2172.
103. Li, M. W., Yudin, A., Vande Voort, C. A., Sabeur, K., Primakoff, P. and Overstreet, J. W., Inhibition of monkey sperm hyaluronidase activity and heterologous cumulus penetration by flavonoids. Biol. Reprod., 1997, 56, 1383-1389.
104. Li, S., Taylor, K. B., Kelly, S. J. and Jedrzejas, M. J., Vitamin C inhibits the enzymatic activity of Streptococcus pneumoniae hyaluronate lyase. J. Biol. Chem., 2001, 276, 15125-15130.
105. Hwang, J., Peterson, H., Hodis, H. N., Choi, B. and Sevanian, A., Ascorbic acid enhances 17B estradial-mediated inhibition of oxidized low density lipoprotein formation. Atherosclerosis, 2000, 150, 275-284.
106. Kalka, K., Mukhtar, H., Turowski-Warke, A. and Merk, H., Biomelanin antioxidants in cosmetics: Assessment based on inhibition of lipid peroxidaton. Skin Pharmacol. Appl. Skin Physiol., 2000, 23, 209-216.
107. Fair, C., Menzel, J., Seeberger, J. and Schweigle, B., Klinische Pharmakologie undanwendungsmoglichkeiten von hyaluronidase unter berucksichtigung von hylase dessau. Wien. Med. Wochenschr., 1997, 147, 1-8.
108. Hubbard, W. C. et al., Intraocular pressure and outflow facility are unchanged following acute and chronical intracameral chondroitinase ABC and hyaluronidase in monkeys. Exp. Eye Res., 1997, 65, 177-190.
109. Fechner, P. U. and Wichmann, W. J., Intraocular use of hyaluronidase to dissolve sodium hyaluronic acid. Refract. Surg., 1997, 13, 502-503.
110. Harooni, M., McMillan, T. and Refojo, M. J., Efficacy and safety of enzymatic posterior vitreous detachment by intravitreal injection of hyaluronidase. Refract. Surg. Dis., 1998, 18, 16-22.
111. West, D. C., Shaw, D. M., Lorenz, P., Adzick, N. S. and Longaker, M. T., Fibrotic healing of adult and late gestation fetal wounds correlates with increased hyaluronidase activity and removal of hyaluronan. J. Biochem. Cell. Biol., 1997, 29, 201-210.
112. Linker, A., Hoffman, P. and Meyer, K., The production of unsaturated uronics by bacterial hyaluronidases. J. Biol. Chem., 1956, 219, 13-25.
113. Sayle, R. A. and Milner-White, E. J., Rasmol: Biomolecular graphics for all. Trends Biochem. Sci., 1995, 20, 374-76.
114. Nicholls, A., GRASP, Graphical representation and analysis of surface potential properties, Columbia University, New York, 1995.