Abstract：
:The major merozoite-piroplasm surface antigen (mMPSA) of Theileria annulata, Tams1, is known to be antigenically diverse. The possession of variable N-linked glycosylation sites and removal of monoclonal antibody 5E1 reactivity by mild periodate treatment suggested, previously, that divergent epitopes may be conferred by secondary modification. This study has shown that monoclonal antibody 5E1 and polyspecific antisera raised against the native protein react against divergent amino acid epitopes that are dependent on a molecular conformation that is sensitive to periodate. Therefore, no experimental evidence exists to confirm the sequence prediction that Tams1 undergoes N-linked glycosylation. Data is also presented indicating that the conformation of the antigen results in presentation of divergent regions on the external surface of the molecule, while conserved regions are more likely to be internal and hidden. In addition, non-reducing SDS-PAGE analysis demonstrated that Tams1 can undergo molecular association to form homo-dimers, trimers and multimers. The potential influence of tertiary structure and inter-molecular association on Tams1 diversity and function is discussed.
journal_name
Mol Biochem Parasitoljournal_title
Molecular and biochemical parasitologyauthors
Katzer F,McKellar S,Ferguson MA,d'Oliveira C,Shiels BRdoi
10.1016/s0166-6851(02)00078-6subject
Has Abstractpub_date
2002-06-01 00:00:00pages
55-67issue
1eissn
0166-6851issn
1872-9428pii
S0166685102000786journal_volume
122pub_type
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journal_title：Molecular and biochemical parasitology
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