E. Detmer et al., THE TRYPANOSOMA-BRUCEI AUTOANTIGEN I 6 IS AN INTERNALLY REPETITIVE CYTOSKELETAL PROTEIN/, European journal of cell biology, 72(4), 1997, pp. 378-384
Self-reactive host antibodies were shown earlier to exhibit strong and
specific cross-reactivity to a particular trypanosomal antigen, prote
in I/6. The current study presents the molecular characterization of p
rotein I/6. The major structural component of the cell body cytoskelet
on of Trypanosoma brucei is a cagelike array of tightly connected micr
otubules which is in close contact to the overlaying cell membrane. Ma
ny of the unususal properties of the cytoskeleton of trypanosomes are
due to the proteins associated with these microtubules. Protein I/6 wa
s now shown to be a microtubule-associated protein, and it may be invo
lved in crosslinking microtubules. Protein I/6 is coded for by a singl
e gene, representing an exception rather than tile rule for trypanosom
al gene organization. From this single gene, two distinct mRNAs are ge
nerated through differential splicing. They differ in their polyadenyl
ation sites, but both code for an identical polypeptide sequence of 33
kDa, Protein I/6 contains a non-functional EF-hand calcium binding do
main and a domain of six tandemly arranged repeat units of eight amino
acids length.