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Infection and Immunity, September 1998, p. 4268-4273, Vol. 66, No. 9
Critical Care Medicine Department, Clinical
Center, National Institutes of Health, Bethesda, Maryland 20892
Received 12 March 1998/Returned for modification 7 May
1998/Accepted 23 June 1998
To facilitate studies of Pneumocystis carinii
infection in humans, we undertook to better characterize and
to express the major surface glycoprotein (MSG) of human P. carinii, an important protein in host-pathogen interactions.
Seven MSG genes were cloned from a single isolate by PCR or genomic
library screening and were sequenced. The predicted proteins, like rat
MSGs, were closely related but unique variants, with a high level of
conservation among cysteine residues. A conserved immunodominant region
(of approximately 100 amino acids) near the carboxy terminus was
expressed at high levels in Escherichia coli and used in
Western blot studies. All 49 of the serum samples, which were taken
from healthy controls as well as from patients with and without
P. carinii pneumonia, were reactive with this peptide by
Western blotting, supporting the hypothesis that most adult humans have
been infected with P. carinii at some point. This
recombinant MSG fragment, which is the first human P. carinii antigen available in large quantities, may be a useful
reagent for investigating the epidemiology of P. carinii
infection in humans.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Characterization of Major Surface Glycoprotein Genes of
Human Pneumocystis carinii and High-Level Expression of
a Conserved Region

*
Corresponding author. Mailing address: Building 10, Room 7D43, 10 Center Dr., MSC 1662, Bethesda, MD 20892-1662. Phone:
(301) 496-9907. Fax: (301) 402-1213. E-mail: jkovacs{at}nih.gov.
Present address: Merck Research Laboratories, Dept. of Drug
Metabolism, West Point, PA 19486-0004.
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