The role of transferrin-receptor variation in the host range of Trypanosoma brucei
Article Abstract:
It has been possible to find a new explanation for transferrin receptor (Tf-R) variability. Minor differences between Tf-Rs can have a significant impact on the binding affinity for transferrins from different mammals. These differences also affect the ability of trypanosomes to grow in the sera of these mammals. The unicellular parasite Trypanosoma brucei has colonized a wide range of mammals and has thus been obliged to find a way of taking up different transferrins effectively without encountering difficulties with the anti-Tf-R antibodies that arise in a chronic infection. It seems that the trypanosome has created a separate high-affinity receptor for different groups of mammals.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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A structural motif in the variant surface glycoproteins of Trypanosoma brucei
Article Abstract:
A study of the structure of the variant surface glycoproteins (VSG) of Trypanosoma brucei is reported. T. brucei is a parasitic protozoan which causes the African sleeping sickness in Hhumans and nagana in cattle. X-ray crystallography analysis showed that VSG ILTat 1.24 resembles the structure of VSG MITat 1.2, although the similarity between their sequences is low. Substitution of carbohydrate for an alpha-helix and other structural similarities with other VSG sequences were also observed. These results suggest that antigenic variation in Trypanosomes is achieved by varying VSG sequences while conserving gross structure.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus
Article Abstract:
The crystal structure of the haemagglutinin-esterase-fusion (HEF) envelope glycoprotein of influenza C is reported. The receptor-binding site and the receptor-destroying enzyme sites have been identified, using receptor analogues. The esterase domain is similar in structure to the Streptomyces scabies esterase, and the stem domain is similar to influenza A haemagglutinin.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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