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Infection and Immunity, February 2006, p. 1189-1195, Vol. 74, No. 2
0019-9567/06/$08.00+0 doi:10.1128/IAI.74.2.1189-1195.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Denise M. Toney,2
Rebecca C. MacLean,1 and
Francine Marciano-Cabral1*
Department of Microbiology and Immunology, Virginia Commonwealth University School of Medicine, Richmond, Virginia 23298,1 Virginia Division of Consolidated Laboratory Services, Richmond, Virginia 232192
Received 15 August 2005/ Returned for modification 17 September 2005/ Accepted 23 November 2005
Naegleria fowleri, the causative agent of primary amebic meningoencephalitis, is resistant to complement lysis. The presence of a complement regulatory protein on the surface of N. fowleri was investigated. Southern blot and Northern blot analyses demonstrated hybridization of a radiolabeled cDNA probe for CD59 to genomic DNA and RNA, respectively, from pathogenic N. fowleri. An 18-kDa immunoreactive protein was detected on the membrane of N. fowleri by Western immunoblot and immunofluorescence analyses with monoclonal antibodies for human CD59. Complement component C9 immunoprecipitated with the N. fowleri "CD59-like" protein from amebae incubated with normal human serum. In contrast, a gene or protein similar to CD59 was not detected in nonpathogenic, complement-sensitive N. gruberi amebae. Collectively, our studies suggest that a protein reactive with antibodies to human CD59 is present on the surface of N. fowleri amebae and may play a role in resistance to lysis by cytolytic proteins.
Present address: Virginia Division of Consolidated Laboratory Services, Richmond, VA 23219.
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