The UDP-glycosyltransferase gene family has expanded differently in Leishmaniinae and Trypanosoma

What is it about?

UDP-glycosyltransferases are transferases involved in adding sugars to proteins that are expressed in the parasite's surface. As surface proteins are the first line of interaction with the host immune system, they are preferred targets for the understanding of host:parasite biology and the development of vaccines and therapeutics. In this paper, we show that the UDP-glycosyltransferase gene family has expanded considerably in both Leishmaniinae and Trypanosoma parasites relative to their free-living ancestor. However, despite needing to meet their superficially common need to decorate their cell surfaces for infection and transmission , they have done so independently. Besides, we show that developmental regulation has been a strong driver of this diversification in both African trypanosomes and Leishmaniinae.

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Why is it important?

We find that seven lineages underline the UDP-glycosyltransferases repertoire in African trypanosomes, whilst the Leishmania UDP-glycosyltransferases repertoire derives from an ancestral tandem array. We also argue that UDP-glycosyltransferases conserved across Leishmania probably encode functionally distinct and non-redundant enzymes, but African trypanosomes sub-telomeric UDP-glycosyltransferases may have expanded to increase numbers of functionally redundant isoforms. Therefore, the different evolution signatures can be used to guide functional studies.

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