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Journal of Clinical Microbiology, April 1998, p. 949-954, Vol. 36, No. 4
0095-1137/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification and Purification of Specific Penicillium marneffei Antigens and Their Recognition by Human Immune Sera

L. Jeavons,1,* A. J. Hamilton,1 N. Vanittanakom,2 R. Ungpakorn,3 E. G. V. Evans,4 T. Sirisanthana,5 and R. J. Hay1

Dermatology Laboratory, St. John's Institute of Dermatology, Thomas Guy House, Guy's Hospital, London SE1-9RT,1 and Department of Microbiology, University of Leeds, Leeds, LS2,4 United Kingdom, and Department of Microbiology2 and Department of Medicine,5 Chiang Mai University Hospital, Chiang Mai 50200, and Institute of Dermatology, Bangkok,3 Thailand

Received 27 October 1997/Returned for modification 2 December 1997/Accepted 10 January 1998

Disseminated infection with the dimorphic pathogenic fungus Penicillium marneffei is increasingly seen among patients with AIDS in southeast Asian countries. Previous studies have demonstrated the presence of humoral immune responses to this fungus in patient sera; we have confirmed this work using sera from P. marneffei-infected patients (n = 21) to develop Western blots of P. marneffei cytoplasmic yeast antigen (CYA). P. marneffei CYA was then partially purified by liquid isoelectric focusing, and fractions were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Immunoenzyme development of the Western blots with pooled sera from patients with P. marneffei infection and with pooled sera from patients with aspergillosis (n = 20), candidiasis (n = 10), cryptococcosis (n = 9), and histoplasmosis (n = 11) revealed three antigens with relative molecular masses of 61, 54, and 50 kDa. These antigens were specifically recognized by the pooled sera from the P. marneffei-infected patients. The 61- and 54-kDa antigens were subsequently purified to homogeneity by preparative gel electrophoresis, and the 50-kDa antigen was partially purified by the same technique. N-terminal amino acid sequencing revealed that the 61-kDa antigen had a strong homology (87% identity) with the antioxidant enzyme catalase. The three antigens were then subjected to SDS-PAGE and Western blotting and to immunoenzyme development with individual patient sera; sera from 86% of P. marneffei-infected patients recognized the 61-kDa antigen, sera from 71% recognized the 54-kDa antigen, and sera from 48% recognized the 50-kDa antigen. These specifically recognized antigens are the first to be purified from P. marneffei and can be used either singly or in combination to detect antibody responses in a large percentage of individuals infected with P. marneffei.

* Corresponding author. Mailing address: Dermatology Laboratory, St. John's Institute of Dermatology, 5th Floor, Thomas Guy House, Guy's Hospital, London SE1-9RT, United Kingdom. Phone: 0171 955 4663. Fax: 0171 407 6689. E-mail: l.jeavons{at}umds.ac.uk.

Journal of Clinical Microbiology, April 1998, p. 949-954, Vol. 36, No. 4
0095-1137/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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