Recurrent expansions of B30.2-associated immune receptor families in fish.

Immunogenetics

Université Paris-Saclay, INRAE, UVSQ, Virologie et Immunologie Moléculaires, 78350, Jouy-en-Josas, France.

Published: February 2022

B30.2 domains, also known as PRY/SPRY, are key components of specific subsets of two large families of proteins involved in innate immunity: the tripartite motif proteins (TRIMs) and the Nod-like receptors (NLRs). TRIM proteins are important, often inducible factors of antiviral innate immunity, targeting multiple steps of viral cycles through a variety of mechanisms. NLRs prime and regulate systemic innate defenses, especially against bacteria, and control inflammation. Large TRIM and NLR subsets characterized by the presence of a B30.2 domain have been reported from a few fish species including zebrafish and seem to be strongly prone to gene duplication/expansion. Here, we performed a large-scale survey of these receptors across about 150 fish genomes, focusing on ray-finned fishes. We assessed the number and genomic distribution of domains and domain combinations associated with TRIMs, NLRs, and other genes containing B30.2 domains and looked for gene expansion patterns across fish groups. We then used a model to test the impact of taxonomy, genome size, and environmental variables on the copy numbers of these genes. Our findings reveal novel domain structures, clade-specific gains and losses. They also assist with the timing of the gene expansions, reveal patterns associated with the MHC, and lay the groundwork for further studies delving deeper into the forces that drive the copy number variation of immune genes on a species level.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00251-021-01235-4DOI Listing

Publication Analysis

Top Keywords

b302 domains
8
innate immunity
8
recurrent expansions
4
expansions b302-associated
4
b302-associated immune
4
immune receptor
4
receptor families
4
fish
4
families fish
4
fish b302
4

Similar Publications

Responsive infant feeding is a critical component of childhood obesity prevention. However, there is little guidance for caregivers on how to do this successfully. The first step to developing an intervention to promote responsive feeding is to systematically identify its barriers and enablers.

View Article and Find Full Text PDF

Genetically determined recurrent fevers.

Curr Opin Immunol

October 2001

Génétique et Physiopathologie des Maladies Inflammatoires, Institut National de la Santé et de la Recherche Médicale (INSERM) EMI 00-05, Faculté de Médecine Cochin Port-Royal, 24 rue du fg St Jacques, 75014, Paris, France.

The usefulness of molecular diagnosis is now well established for genetically determined recurrent fevers. In familial Mediterranean fever, the severity of the disease and the risk of renal amyloidosis are correlated with mutations in MEFV, and the serum amyloid-associated protein (SAA)1 alpha/alpha allele is a modifying factor for amyloidosis. Study of the genes in various species shows that the human mutations represent a reappearance of the ancestral amino acid state and the B30-2 domain, where most human mutations are localized, is absent in the rat and mouse proteins.

View Article and Find Full Text PDF

Analysis of 600 kb of sequence encompassing the beta-prime adaptin (BAM22) gene on human chromosome 22 revealed intrachromosomal duplications within 22q12-13 resulting in three active RFPL genes, two RFPL pseudogenes, and two pseudogenes of BAM22. The genomic sequence of BAM22vartheta1 shows a remarkable similarity to that of BAM22. The cDNA sequence comparison of RFPL1, RFPL2, and RFPL3 showed 95%-96% identity between the genes, which were most similar to the Ret Finger Protein gene from human chromosome 6.

View Article and Find Full Text PDF

During a search for novel coding sequences within the human MHC class I region (chromosome 6p21.3), we found an exon (named B30-2) coding for a 166-amino-acid peptide which is very similar to the C-terminal domain of several coding sequences: human 52-kD Sjögren's syndrome nuclear antigen A/Ro (SS-A/Ro) and ret finger protein (RFP), Xenopus nuclear factor 7 (XNF7), and bovine butyrophilin. The first three of these proteins share similarities over the whole length of the molecule whereas butyrophilin is similar in the C-terminal domain.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!