Characterization of an Aspergillus flavus alkaline protease and its role in the infection of maize kernels

Toxin Reviews

Volumn 28, Issue 2-3, 2009, Pages 187-197

  Chen, Zhi Yuan ^a   Brown, Robert L ^b   Cary, Jeffrey W ^b   Damann, Kenneth E ^a   Cleveland, Thomas E ^b  

^a LOUISIANA STATE UNIVERSITY   (United States)

^b SOUTHERN REGIONAL RESEARCH CENTER   (United States)

Author keywords

Aflatoxin contamination; Alkaline protease; Aspergillus flavus; Corn; Infection; Substrate dependent production

Indexed keywords

AFLATOXIN; ALKALINE PROTEINASE; BENZYLSULFONYL FLUORIDE; GELATIN; GLUCOSE; STARCH; TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS FLAVUS; CONTROLLED STUDY; CULTURE MEDIUM; DNA SEQUENCE; EMBRYO; ENZYME ACTIVITY; FUNGAL PLANT DISEASE; FUNGUS CULTURE; MAIZE; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; SEED KERNEL;

ASPERGILLUS; ASPERGILLUS FLAVUS; SOLANUM TUBEROSUM; ZEA MAYS;

EID: 72149121091     PISSN: 15569543     EISSN: 15569551     Source Type: Journal    
DOI: 10.1080/15569540903089221     Document Type: Article

References (49)

1. Adye JC, Mateles RI. (1964). Incorporation of labelled compounds into aflatoxins. Biochim Biophys Acta. 86: 418-420.
2. Alexandrov NN, Brover VV, Freidin S, Troukhan ME, Tatarinova TV, Zhang H, Swaller TJ, Lu YP, Bouck J, Flavell RB, Feldmann KA. (2009). Insights into corn genes derived from large-scale cDNA sequencing. Plant Mol Biol. 69: 179-194.
3. Bradford MM. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72: 248-254.
4. Brown RL, Cleveland TE, Cotty PJ, Mellon JE. (1992). Spread of Aspergillus flavus in cotton bolls, decay of intercarpellary membranes, and production of fungal pectinases. Phytopathology. 82: 462-467.
5. Brown RL, Cleveland TE., Payne GA, Woloshuk CP, Campbell KW, White DG. (1995). Determination of resistance to aflatoxin production in maize kernels and detection of fungal colonization using an Aspergillus flavus transformant expressing Escherichia coli ?pound;-glucuronidase. Phytopathology. 85: 983-989.
6. Brown RL, Cotty PJ, Cleveland TE, Widstrom NW. (1993). Living maize embryo influences accumulation of aflatoxin in maize kernels. J Food Prot. 56: 967-971.
7. Cheevadhanarak S, Renno DV, Saunders G, Holt G. (1991). Cloning and selective overexpression of an alkaline protease-encoding gene from Aspergillus oryzae. Gene. 108: 151-155.
8. Chen Z-Y, Brown RL, Lax AR, Cleveland TE, Russin JS. (1999a). Inhibition of plant-pathogenic fungi by a corn trypsin inhibitor overexpressed in Escherichia coli. Appl Environ Microbiol. 65: 1320-1324.
9. Chen Z-Y, Brown RL, Lax AR, Guo BZ, Cleveland TE, Russin JS. (1998). Resistance to Aspergillus flavus in corn kernels is associated with a 14 kDa protein. Phytopathology. 88: 276-281.
10. Chen Z-Y, Brown RL, Russin JS, Lax AR, Cleveland TE. (1999b). A corn trypsin inhibitor with antifungal activity inhibits Aspergillus flavus cent;-amylase. Phytopathology. 89: 902-907.
11. Chen Z-Y, Lavigne LL, Mason CB, Moroney JV. (1997). Cloning and overexpression of two cDNAs encoding the low- CO2-inducible chloroplast envelope protein LIP-36 from Chlamydomonas reinhardtii. Plant Physiol. 114: 265-273.
12. Cleveland TE, Cotty PJ. (1991). Invasiveness of Aspergillus flavus isolates in wounded cotton bolls is associated with production of a specific fungal polygalacturonase. Phytopathology. 81: 155-158.
13. Cotty PJ. (1989). Virulence and cultural characteristics of two Aspergillus flavus strains pathogenic on cotton. Phytopathology. 79: 808-814.
14. Cotty PJ, Cleveland TE, Brown RL, Mellon JE. (1990). Variation in polygalacturonase production among Aspergillus flavus isolates. Appl Environ Microbiol. 56: 3885-3887.
15. Dean RA, Timberlake WE. (1989). Production of cell wall- degrading enzymes by Aspergillus nidulans: a model system for fungal pathogenesis of plants. Plant Cell. 1: 265-273.
16. Dobinson KF, Lecomte N, Lazarovits G. (1997). Production of an extracellular trypsin-like protease by the fungal plant pathogen Verticillium dahliae. Can J Microbiol. 43: 227-233.
17. Guo BZ, Russin JS, Cleveland TE, Brown RL, Widstrom NW. (1996). Resistance to aflatoxin contamination in corn as influenced by relative humidity and kernel germination. J Food Prot. 59: 276-281.
18. Gupta SC, Leathers TD, Wicklow DT. (1993). Hydrolytic enzymes secreted by Paecilomyces lilacinus cultured on sclerotia of Aspergillus flavus. Appl Microbiol Biotechnol. 39: 99-103.
19. Hanzi M, Shimizu M, Hearn VM, Monod M. (1993). A study of the alkaline proteases secreted by different Aspergillus species. Mycoses. 36: 351-356.
20. Hislop EC, Paver JL, Keon JPR. (1982). An acid protease produced by Monilinia fructigena in vitro and in infected apple fruits, and its possible role in pathogenesis. J Gen Microbiol. 128: 799-807.
21. Impoolsup A, Bhumiratana A, Flegel TW. (1981). Isolation of alkaline and neutral proteases from Aspergillus flavus var. columnaris, a soy sauce Koji mold. Appl Environ Microbiol. 42: 619-628.
22. Jurkova J, Mikes O. (1971). Stability of alkaline protease from Aspergillus flavus. Collection Czechoslov Chem Commun. 36: 2739-2743.
23. Kapat A, Zimand G, Elad Y. (1998). Effect of two isolates of Trichoderma harzianum on the activity of hydrolytic enzymes produced by Botrytis cinerea. Physiol Mol Plant Path. 52: 127-137.
24. Katz ME, Rice RN, Cheetham BF. (1994). Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease. Gene. 150: 287-292.
25. Keller NP, Butchko RAE, Sarr B, Phillips TD. (1994). A visual pattern of mycotoxin production in maize kernels by Aspergillus spp. Phytopathology. 84: 483-488.
26. Kikot GE, Hours RA, Alconada TM. (2008). Contribution of cell wall degrading enzymes to pathogenesis of Fusarium graminearum: a review. J Basic Microbiol. 48: 1-11.
27. Laemmli UK. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227: 680-685.
28. Malathi S, Chakraborty R. (1991). Production of alkaline protease by a new Aspergillus flavus isolate under solid-substrate fermentation conditions for use as a depilation agent. Appl Environ Microbiol. 57: 712-716.
29. Mellon JE, Cotty PJ. (1995). Expression of elastinolytic activity among isolates in Aspergillus Section Flavi. Mycopathologia. 131: 115-120.
30. Mellon JE, Cotty PJ. (1996). Purification and partial characterization of an elastinolytic proteinase from Aspergillus flavus culture filtrates. Appl Microbiol Biotechnol. 46: 138-142.
31. Mikes O, Turkova J, Allen G, Toan NB. (1980). Isolation and structure determination of the peptides from the chymotryptic hydrolysate of the alkaline protease from Aspergillus flavus. Collection Czechoslov Chem Commun. 45: 1996-2028.
32. Misaki T, Yamada M, Okazaki T, Sawada J. (1970). Studies on the protease constitution of Aspergillus oryzae. I. Systematic separation and purification of proteases. Agric Biol Chem. 34: 1383-1392.
33. Murakami K, Ishida Y, Masaki A, Tatsumi H, Murakami S, Nakano E, Motai H, Kawabe H, Arimura H. (1991). Isolation and characterization of the alkaline protease gene of Aspergillus oryzae. Agric Biol Chem. 55: 2807-2811.
34. Nakadai T, Nasuno S, Iguchi N. (1973). Purification and properties of alkaline proteinase from Aspergillus oryzae. Agric Biol Chem. 37: 2685-2694.
35. Ramesh MV, Sirakova T, Kolattukudy PE. (1994). Isolation, characterization, and cloning of cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus. Infect Immun. 62: 79-85.
36. Rauscher M, Mendgen K, Deising H. (1995). Extracellular proteases of the rust fungus Uromyces viciae-fabae. Exp Mycol. 19: 26-34.
37. Rhodes JC. (1995). Aspergillus proteinases and their interactions with host tissues. Can J Bot. 73: S1126-S1131.
38. Robertsen B. (1984). An alkaline extracellular protease produced by Cladosporium cucumerinum and its possible importance in the development of scab disease of cucumber seedlings. Physiol Plant Pathol. 24: 83-92.
39. Ryan CA. (1973). Proteolytic enzymes and their inhibitors in plants. Annu Rev Plant Physiol. 24: 173-196.
40. Shieh MT, Brown RL, Whitehead MP, Cary JW, Cotty PJ, Cleveland TE, Dean RA. (1997). Molecular genetic evidence for the involvement of a specific polygalacturonase, P2c, in the invasion and spread of Aspergillus flavus in cotton bolls. Appl Environ Microbiol. 63: 3548-3552.
41. Smith JM, Tang CM, Van Noorden S, Holden DW. (1994). Virulence of Aspergillus fumigatus double mutants lacking restriction and an alkaline protease in a low-dose model of invasive pulmonary aspergillosis. Infect Immun. 62: 5247-5254.
42. Swegel M, Kramer KJ, Muthukrishnan S. (1992). Properties of barley seed chitinases and release of embryo-associated isoforms during early stages of imbibition. Plant Physiol. 99: 1009-1014.
43. Tang CM, Cohen J, Krausz T, Van Noorden S, Holden DW. (1993). The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect. Immun. 61: 1650-1656.
44. Tatsumi H, Ohsawa M, Tsuji RF, Murakami S, Nakano E, Motai H, Masaki A, Ishida Y, Murakami K, Kawabe H, Arimura H. (1988). Cloning and sequencing of the alkaline protease cDNA from Aspergillus oryzae. Agric Biol Chem. 52: 1887-1888.
45. Turkova J, Mikes O, Gancev K, Boublik M. (1969). Isolation and characterization of alkaline proteinase of Aspergillusflavus. Biochim Biophys Acta. 178: 100-111.
46. Widstrom NW, McMillian WW, Wilson DM. (1987). Segregation for resistance to aflatoxin contamination among seeds on an ear of hybrid maize. Crop Sci. 27: 961-963.
47. Wilson CM. (1987). Proteins of the kernel. In: Watson SA, Ramstad PE, eds. Corn: Chemistry and Technology. St. Paul, MN: American Association of Cereal Chemists, Inc., pp. 273-310.
48. Woloshuk CP, Cavaletto JR, Cleveland TE. (1997). Inducers of aflatoxin biosynthesis from colonized maize kernels are generated by an amylase activity from Aspergillus flavus. Phytopathology. 87: 164-169.
49. Yu CJ, Chiou SH, Lai WY, Chiang BL, Chow LP. (1999). Characterization of a novel allergen, a major IgE-binding protein from Aspergillus flavus, as an alkaline serine protease. Biochem Biophys Res Commun. 261: 669-675.