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Molecular evolution and in vitro characterization of Botryllus histocompatibility factor
Daryl A Taketa1, Marie L Nydam2, Adam D Langenbacher1
1Department of Molecular, Cellular and Developmental Biology, University of California-Santa Barbara, Santa Barbara, CA, 93106, USA.
Immunogenetics
|September 12, 2015
Summary
Botryllus schlosseri uses the fuhc locus for colony fusion. A newly identified factor, bhf, shows low polymorphism and may act as a scaffolding protein rather than a direct allorecognition determinant.
Area of Science:
- Marine biology
- Immunology
- Genetics
Background:
- Botryllus schlosseri colonies fuse by sharing fuhc locus alleles.
- Incompatibility leads to inflammatory responses and melanin scar formation.
- The molecular basis of allorecognition in B. schlosseri is not fully understood.
Purpose of the Study:
- To characterize the Botryllus histocompatibility factor (bhf), a candidate allodeterminant.
- To investigate the polymorphism, isoforms, expression, and localization of bhf.
- To hypothesize the function of bhf in allorecognition.
Main Methods:
- DNA and protein analysis of bhf.
- mRNA-Seq and EST assembly for isoform identification.
- Whole-mount fluorescent in situ hybridization.
- HEK293T cell transfection for protein localization studies.
Main Results:
- Bhf exhibits low polymorphism and lacks typical selection patterns.
- A truncated bhf isoform lacking exon 3 was identified.
- Bhf is co-expressed with cfuhc(sec) in a subset of cells.
- BHF localizes to the cytoplasm and nucleus in HEK293T cells.
Conclusions:
- Bhf's low polymorphism and localization suggest it may not be a direct allorecognition determinant.
- Bhf might function as a scaffolding protein within a larger complex.
- Further research is needed to elucidate bhf's precise role in B. schlosseri allorecognition.
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