Pm. Jacquinot et al., NATURE OF CANDIDA-ALBICANS-DERIVED CARBOHYDRATE ANTIGEN RECOGNIZED BYA MONOCLONAL-ANTIBODY IN PATIENT SERA AND DISTRIBUTION OVER CANDIDA SPECIES, FEMS microbiology letters, 169(1), 1998, pp. 131-138
The minimal epitope of an anti-Candida albicans mannan monoclonal anti
body (MAb) EB-CA1, used to detect mannanemia in patient sera, was dete
rmined. MAb EB-CA1 exhibited reactivity with oligomannosides released
from the mannan acid stable domain, converted into neoglycolipids (NGL
s) and coated onto ELISA plates. Reactivity occurred with mannopentaos
e and higher oligomers, whereas mannotriose and mannotetraose were unr
eactive. MAb EB-CA1 binding to mannan acid stable mannopentaose NGL di
splayed a dose dependent and saturable specific reactivity curve where
as there was a complete absence of binding, even at high concentration
s, with NGLs constructed from the beta-1,2-linked mannopentaose derive
d from the mannan acid labile fraction. MAb EB-CA1 binding to acid sta
ble mannopentaose NGL was inhibited by the homologous oligomannoside b
ut not by mannotriose and mannotetraose. NMR analysis showed that mann
otriose and mannotetraose contained exclusively alpha-1,2-linked D-man
nopyranose units and that mannopentaose was a mixture of a mannopentao
se alpha-1,2-linked and an isomer in which the fifth mannose was alpha
-1,6-linked to the reducing unit of manno-alpha-1,2 tetraose. Western
blot analysis has shown that MAb EB-CA1 epitope was expressed on a wid
e range of C. albicans manno-glycoconjugate as well as on manno-glycoc
onjugates of other pathogenic species of the genus Candida, viz. C. tr
opicalis, C. glabrata, C. parapsilosis and C. krusei. (C) 1998 Federat
ion of European Microbiological Societies. Published by Elsevier Scien
ce B.V. All rights reserved.