Isolation and properties of extracellular proteinases of Penicillium marneffei

References

Andrianopoulos, A. (2002). Control of morphogenesis in the human fungal pathogen Penicillium marneffei. Int. J. Med. Microbiol.292, 331–347.10.1078/1438-4221-00217Search in Google Scholar PubMed

Borneman, A.R., Hynes, M.J., and Andrianopoulos, A. (2002). A basic helix-loop-helix protein with similarity to the fungal morphological regulators, Phd1p, Efg1p and StuA, controls conidiation but not dimorphic growth in Penicillium marneffei. Mol. Microbiol.44, 621–631.10.1046/j.1365-2958.2002.02906.xSearch in Google Scholar PubMed

Boyce, K.J., Hynes, M.J., and Andrianopoulos, A. (2003). Control of morphogenesis and actin localization by the Penicillium marneffei RAC homolog. J. Cell Sci.116, 1249–1260.10.1242/jcs.00319Search in Google Scholar PubMed

Boyce, K.J., Hynes, M.J., and Andrianopoulos, A. (2005). The Ras and Rho GTPases genetically interact to co-ordinately regulate cell polarity during development in Penicillium marneffei. Mol. Microbiol.55, 1487–1501.10.1111/j.1365-2958.2005.04485.xSearch in Google Scholar PubMed

Capponi, M., Segretain, G., and Sureau, P. (1956). [Penicillosis from Rhizomys sinensis.]. Bull. Soc. Pathol. Exot. Filiales49, 418–421.Search in Google Scholar

Chan, Y.H., Wong, K.M., Lee, K.C., Kwok, P.C., Chak, W.L., Choi, K.S., Chau, K.F., and Li, C.S. (2004). Pneumonia and mesenteric lymphadenopathy caused by disseminated Penicillium marneffei infection in a cadaveric renal transplant recipient. Transpl. Infect. Dis.6, 28–32.10.1111/j.1399-3062.2004.00038.xSearch in Google Scholar PubMed

Chariyalertsak, S., Sirisanthana, T., Supparatpinyo, K., Praparattanapan, J., and Nelson, K.E. (1997). Case-control study of risk factors for Penicillium marneffei infection in human immunodeficiency virus-infected patients in northern Thailand. Clin. Infect. Dis.24, 1080–1086.10.1086/513649Search in Google Scholar PubMed

Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T.J., Higgins, D.G., and Thompson, J.D. (2003). Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res.31, 3497–3500.10.1093/nar/gkg500Search in Google Scholar PubMed PubMed Central

Chierakul, W., Rajanuwong, A., Wuthiekanun, V., Teerawattanasook, N., Gasiprong, M., Simpson, A., Chaowagul, W., and White, N.J. (2004). The changing pattern of bloodstream infections associated with the rise in HIV prevalence in northeastern Thailand. Trans. R. Soc. Trop. Med. Hyg.98, 678–686.10.1016/j.trstmh.2004.01.011Search in Google Scholar PubMed

Cooper, C.R. Jr., and Haycocks, N.G. (2000). Penicillium marneffei: an insurgent species among the penicillia. J. Eukaryot. Microbiol.47, 24–28.10.1111/j.1550-7408.2000.tb00006.xSearch in Google Scholar PubMed

Deng, Z.L. and Connor, D.H. (1985). Progressive disseminated penicilliosis caused by Penicillium marneffei. Report of eight cases and differentiation of the causative organism from Histoplasma capsulatum. Am. J. Clin. Pathol.84, 323–327.Search in Google Scholar

Fujinaga, M., Cherney, M.M., Oyama, H., Oda, K., and James, M.N. (2004). The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum. Proc. Natl. Acad. Sci. USA101, 3364–3369.10.1073/pnas.0400246101Search in Google Scholar PubMed PubMed Central

Iadarola, P., Lungarella, G., Martorana, P.A., Viglio, S., Guglielminetti, M., Korzus, E., Gorrini, M., Cavarra, E., Rossi, A., Travis, J., and Luisetti, M. (1998). Lung injury and degradation of extracellular matrix components by Aspergillus fumigatus serine proteinase. Exp. Lung. Res.24, 233–251.10.3109/01902149809041532Search in Google Scholar

Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature227, 680–685.10.1038/227680a0Search in Google Scholar

Matsudaira, P. (1987). Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem.262, 10035–10038.10.1016/S0021-9258(18)61070-1Search in Google Scholar

Monod, M., Capoccia, S., Lechenne, B., Zaugg, C., Holdom, M., and Jousson, O. (2002). Secreted proteases from pathogenic fungi. Int. J. Med. Microbiol.292, 405–419.10.1078/1438-4221-00223Search in Google Scholar

Moon, J.L., Banbula, A., Oleksy, A., Mayo, J.A., and Travis, J. (2001). Isolation and characterization of a highly specific serine endopeptidase from an oral strain of Staphylococcus epidermidis. Biol. Chem.382, 1095–1099.10.1515/BC.2001.138Search in Google Scholar

Naglik, J.R., Challacombe, S.J., and Hube, B. (2003). Candida albicans secreted aspartyl proteinases in virulence and pathogenesis. Microbiol. Mol. Biol. Rev.67, 400–428.10.1128/MMBR.67.3.400-428.2003Search in Google Scholar

Potempa, J., Banbula, A., and Travis, J. (2000). Role of bacterial proteinases in matrix destruction and modulation of host responses. Periodontology24, 153–192.10.1034/j.1600-0757.2000.2240108.xSearch in Google Scholar

Poussereau, N., Creton, S., Billon-Grand, G., Rascle, C., and Fevre, M. (2001). Regulation of acp1, encoding a non-aspartyl acid protease expressed during pathogenesis of Sclerotinia sclerotiorum. Microbiology147, 717–726.10.1099/00221287-147-3-717Search in Google Scholar

Rawlings, N.D., Tolle, D.P., and Barrett, A.J. (2004). MEROPS: the peptidase database. Nucleic Acids Res.32, D160–164.10.1093/nar/gkh071Search in Google Scholar

Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual. 2nd ed. (Plainview, NY, USA: Cold Spring Harbor Laboratory Press).Search in Google Scholar

Schägger, H., and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem.166, 368–379.10.1016/0003-2697(87)90587-2Search in Google Scholar

Todd, R.B., Greenhalgh, J.R., Hynes, M.J., and Andrianopoulos, A. (2003). TupA, the Penicillium marneffei Tup1p homologue, represses both yeast and spore development. Mol. Microbiol.48, 85–94.10.1046/j.1365-2958.2003.03426.xSearch in Google Scholar PubMed

Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA76, 4350–4354.10.1073/pnas.76.9.4350Search in Google Scholar PubMed PubMed Central

Travis, J., Potempa, J., and Maeda, H. (1995). Are bacterial proteinases pathogenic factors? Trends Microbiol.3, 405–407.Search in Google Scholar

Wang, J.L., Hung, C.C., Chang, S.C., Chueh, S.C., and La, M.K. (2003). Disseminated Penicillium marneffei infection in a renal-transplant recipient successfully treated with liposomal amphotericin B. Transplantation76, 1136–1137.10.1097/01.TP.0000088667.02294.E7Search in Google Scholar PubMed

Woo, P.C., Lau, S.K., Lau, C.C., Chong, K.T., Hui, W.T., Wong, S.S., and Yuen, K.Y. (2005). Penicillium marneffei fungaemia in an allogeneic bone marrow transplant recipient. Bone Marrow Transplant.35, 831–833.10.1038/sj.bmt.1704895Search in Google Scholar PubMed

Xi, L.Y, Lu, C.M., Zhou, X.Y., Wang, L.X., and Xie, S.S. (2004). Fifteen cases of penicilliosis in Guangdong, China. Mycopathologia158, 151–155.Search in Google Scholar

Youngchim, S., Hay, R.J., and Hamilton, A.J. (2005). Melanization of Penicillium marneffei in vitro and in vivo. Microbiology151, 291–299.10.1099/mic.0.27433-0Search in Google Scholar PubMed

Zuber, S., Hynes, M.J., and Andrianopoulos, A. (2002). G-protein signaling mediates asexual development at 25°C but has no effect on yeast-like growth at 37°C in the dimorphic fungus Penicillium marneffei. Eukaryot. Cell1, 440–447.10.1128/EC.1.3.440-447.2002Search in Google Scholar PubMed PubMed Central

Zuber, S., Hynes, M.J., and Andrianopoulos, A. (2003). The G-protein α-subunit GasC plays a major role in germination in the dimorphic fungus Penicillium marneffei. Genetics164, 487–499.10.1093/genetics/164.2.487Search in Google Scholar PubMed PubMed Central