alpha-helical coiled-coil structures of Trypanosoma brucei variable surface glycoproteins

We have used electron microscopy to examine purified intact variable surface glycoproteins (VSGs) from clones derived from two distinct stocks of Trypanosoma brucei . The VSG molecule from MITat 1.2 has a large elongated domain consistent with the shape of the dimeric N-terminal domain determined by X-ray analysis (see preceding paper 1 ), and a heretofore unseen short, thin fibrous tail presumed to be the C-terminal domain. Electron microscopy on DiTat 1.3, however, indicates a morphology quite distinct from that of MITat 1.2. Analysis of four VSG amino acid sequences reveals 7-fold periodicities (heptad repeats) which indicate that α -helical coiled-coil secondary structure elements occur in all of these VSGs, consistent with the observation of helical bundles in one VSG 1 . These results suggest the possibility that VSG antigenic diversity may be related to a diversity in length and disposition of α -helical bundles and coiled-coil domains.