Human salivary MUC7 mucin peptides: Effect of size, charge and cysteine residues on antifungal activity

Biochemical Journal

Volumn 375, Issue 1, 2003, Pages 175-182

  Situ, Hongsa ^a   Wei, Guoxian ^a   Smith, Christina J ^a   Mashhoon, Shirin ^a   Bobek, Libuse A ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

Amphipathicity; Candida albicans; Cryptococcus neoformans; MUC7 12 mer; Secondary structure

Indexed keywords

CONFORMATIONS; FLUORESCENCE; FUNGICIDES; MICROORGANISMS; MICROSCOPIC EXAMINATION; MOLECULAR WEIGHT;

THERAPEUTIC AGENTS;

POLYPEPTIDES;

CYSTEINE; HUMAN SALIVARY LOW MOLECULAR MASS MUCIN 7; MUCIN; PEPTIDE; UNCLASSIFIED DRUG; AMINO ACID; ANTIFUNGAL AGENT; MUC7 PROTEIN, HUMAN; SALIVA PROTEIN;

AMINO TERMINAL SEQUENCE; ANTIFUNGAL ACTIVITY; ARTICLE; BACTERIUM; BINDING AFFINITY; CANDIDA ALBICANS; CARBOXY TERMINAL SEQUENCE; CELL ASSAY; CELL KILLING; CELL MEMBRANE POTENTIAL; CONTROLLED STUDY; CORRELATION ANALYSIS; CRYPTOCOCCUS NEOFORMANS; DRUG CONFORMATION; DRUG EFFECT; DRUG POTENCY; DRUG SCREENING; DRUG SYNTHESIS; FLUORESCENCE MICROSCOPY; FUNGAL CELL; MEASUREMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; SEQUENCE ANALYSIS; AMINO ACID SEQUENCE; CHEMISTRY; CIRCULAR DICHROISM; DOSE RESPONSE; ELECTRICITY; HUMAN; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE;

BACTERIA (MICROORGANISMS); CANDIDA; CANDIDA ALBICANS; FILOBASIDIELLA NEOFORMANS;

AMINO ACID SEQUENCE; AMINO ACIDS, BASIC; ANTIFUNGAL AGENTS; CANDIDA ALBICANS; CIRCULAR DICHROISM; CRYPTOCOCCUS NEOFORMANS; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROSTATICS; HUMANS; MEMBRANE POTENTIALS; MOLECULAR SEQUENCE DATA; MUCINS; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SALIVARY PROTEINS;

EID: 0141919277     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030779     Document Type: Article

References (42)

1. Ostrosky-Zeichner, L., Rex, J. H., Bennett, J. and Kullberg, B. J. (2002) Deeply invasive candidiasis. Infect. Dis. Clin. North Am. 16, 821-835
2. Boman, H. G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92
3. Maloy, W. L. and Kari, U. P. (1995) Structure-activity studies on magainins and other host defense peptides. Biopolymers 37, 105-122
4. Epand, R. M. and Vogel, H. J. (1999) Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462, 11-28
5. De Lucca, A. J. (2000) Antifungal peptides: potential candidates for the treatment of fungal infections. Expert Opin. Investig. Drugs 9, 273-299
6. Hancock, R. E. (1997) Peptide antibiotics. Lancet 349, 418-422
7. Zanetti, M., Gennaro, R., Skerlavaj, B., Tomasinsig, L. and Circo, R. (2002) Cathelicidin peptides as candidates for a novel class of antimicrobials. Curr. Pharm. Des. 8, 779-793
8. Scott, M. G. and Hancock, R. E. (2000) Cationic antimicrobial peptides and their multifunctional role in the immune system. Crit. Rev. Immunol. 20, 407-431
9. Shai, Y. (2002) From innate immunity to de novo designed antimicrobial peptides. Curr. Pharm. Des. 8, 715-725
10. Hancock, R. E. and Rozek, A. (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206, 143-149
11. Lehrer, R. I. and Ganz, T. (1999) Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11, 23-27
12. Nibbering, P. H., Danesi, R., van't Wout, J. W., van Dissel, J. T., Senesi, S. and Lupetti, A. (2002) Antimicrobial peptides: therapeutic potential for the treatment of Candida infections. Expert Opin. Investig. Drugs 11, 309-318
13. Sitaram, N. and Nagaraj, R. (1999) Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim. Biophys. Acta 1462, 29-54
14. van't Hof, W., Veerman, E. C., Helmerhorst, E. J. and Amerongen, A. V. (2001) Antimicrobial peptides: properties and applicability. Biol. Chem. 382, 597-619
15. Sitaram, N. and Nagaraj, R. (2002) The therapeutic potential of host-defense antimicrobial peptides. Curr. Drug Targets 3, 259-267
16. Andreu, D. and Rivas, L. (1998) Animal antimicrobial peptides: an overview. Biopolymers 47, 415-433
17. Bobek, L. A. and Situ, H. (2003) MUC7 20-mer: investigation of antimicrobial activity, secondary structure and possible mechanism of antifungal action. Antimicrob. Agents Chemother. 47, 645-652
18. Bobek, L. A., Mashhoon, S. and Situ, H. (2002) Human salivary MUC7 mucin peptides: effect of size, charge, and cysteine residues on antifungal activity. J. Dent. Res. 81, 236
19. Zasloff, M. (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. U.S.A. 84, 5449-5453
20. Nosanchuk, J. D. and Casadevall, A. (1997) Cellular charge of Cryptococcus neoformans: contributions from the capsular polysaccharide, melanin, and monoclonal antibody binding. Infect. Immun. 65, 1836-1841
21. Rothstein, D. M., Spacciapoli, P., Tran, L. T., Xu, T., Roberts, F. D., Dalla Serra, M., Buxton, D. K., Oppenheim, F. G. and Friden, P. (2001) Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5. Antimicrob. Agents Chemother. 45, 1367-1373
22. Helmerhorst, E. J., van't Hof, W., Breeuwer, P., Veerman, E. C., Abee, T., Troxler, R. F., Amerongen, A. V. and Oppenheim, F. G. (2001) Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation. J. Biol. Chem. 276, 5643-5649
23. Oekonomopulos, R. and Jung, G. (1980) Circular dichroism and conformational analysis of the membrane-modifying peptide N-t-Boc-(Aib-L-Ala)5-Gly-Ala-Aib-Pro-Ala-Aib-Aib-Glu-(OBzl)-Gln-OMe with respect to alamethicin. Biopolymers 19, 203-214
24. Sudha, T. S., Vijayakumar, E. K. and Balaram, P. (1983) Circular dichroism studies of helical oligopeptides. Can 3(10) and α-helical conformations be chiroptically distinguished? Int. J. Pept. Protein Res. 22, 464-468
25. Liu, B., Rayment, S. A., Gyurko, C., Oppenheim, F. G., Offner, G. D. and Troxler, R. F. (2000) The recombinant N-terminal region of human salivary mucin MG2 (MUC7) contains a binding domain for oral Streptococci and exhibits candidacidal activity. Biochem. J. 345, 557-564
26. Ruissen, A. L., Groenink, J., Helmerhorst, E. J., Walgreen-Weterings, E., van't Hof, W., Veerman, E. C. and Nieuw Amerongen, A. V. (2001) Effects of histatin 5 and derived peptides on Candida albicans. Biochem. J. 356, 361-368
27. Wu, M., Maier, E., Benz, R. and Hancock, R. E. (1999) Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38, 7235-7242
28. Levine, M. J. (1993) Salivary macromolecules. A structure/function synopsis. Ann. N.Y. Acad. Sci. 694, 11-16
29. Tabak, L. A. (1995) In defense of the oral cavity: structure, biosynthesis, and function of salivary mucins. Annu. Rev. Physiol. 57, 547-564
30. Tabak, L. A. (1998) Protein structure and function relationships: mucins. In Oral Biology at the Turn of the Century (Guggenheim, B. and Shapiro, S., eds.), pp. 189-197, S. Karger, Basel
31. Schenkels, L. C. P. M., Gururaja, T. L. and Levine, M. J. (1996) Salivary mucins: their role in oral mucosal barrier function and drug delivery. In Oral Mucosal Drug Delivery (Rathbone, M.J., ed.), pp. 191-220, Marcel Dekker, New York
32. Gururaja, T. L., Levine, J. H., Tran, D. T., Naganagowda, G. A., Ramalingam, K., Ramasubbu, N. and Levine, M. J. (1999) Candidacidal activity prompted by N-terminus histatin-like domain of human salivary mucin (MUC7) 1. Biochim. Biophys. Acta 1431, 107-119
33. Satyanarayana, J., Situ, H., Narasimhamurthy, S., Bhayani, N., Bobek, L. A. and Levine, M. J. (2000) Divergent solid-phase synthesis and candidacidal activity of MUC7 D1, a 51-residue histidine-rich N-terminal domain of human salivary mucin MUC7. J. Pept. Res. 56, 275-282
34. Liu, B., Rayment, S. A., Soares, R. V., Oppenheim, F. G., Offner, G. D., Fives-Taylor, P. and Troxler, R. F. (2002) Interaction of human salivary mucin MG2, its recombinant N-terminal region and a synthetic peptide with Actinobacillus actinomycetemcomitans. J. Periodontal Res. 37, 416-424
35. Ueta, E., Tanida, T. and Osaki, T. (2001) A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils. J. Pept. Res. 57, 240-249
36. Bessalle, R., Haas, H., Goria, A., Shalit, I. and Fridkin, M. (1992) Augmentation of the antibacterial activity of magainin by positive-charge chain extension. Antimicrob. Agents Chemother. 36, 313-317
37. Blondelle, S. E. and Houghten, R. A. (1992) Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 31, 12688-12694
38. Dathe, M., Schumann, M., Wieprecht, T., Winkler, A., Beyermann, M., Krause, E., Matsuzaki, K., Murase, O. and Bienert, M. (1996) Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35, 12612-12622
39. Kiyota, T., Lee, S. and Sugihara, G. (1996) Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes. Biochemistry 35, 13196-13204
40. Kwon, M. Y., Hong, S. Y. and Lee, K. H. (1998) Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. Biochim. Biophys. Acta 1387, 239-248
41. Oren, Z. and Shai, Y. (1997) Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36, 1826-1835
42. Feder, R., Dagan, A. and Mor, A. (2000) Structure-activity relationship study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity. J. Biol. Chem. 275, 4230-4238