Broad distribution, high diversity and ancient origin of the ApeC-containing proteins

Li, Yuhui; Li, Jin; Yan, Xinyu; Chen, Shenghui; Wu, Cheng‐Yi; Huang, Huiqing; Shi, Yi; Huang, Guangrui; Dong, Meiling; Xu, Anlong; Huang, Shengfeng

doi:10.1016/j.ympev.2020.107009

Cited by 10 publications

(19 citation statements)

References 27 publications

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“…Amphioxus ACP genes were identified in the B. floridae genome from the Joint Genome Institute (JGI, http://genome.jgi-psf.org/ Brafl1/Brafl1.home.html) database in our previous work (2). Using these sequences as baits, we blasted the transcript database of B. floridae (http://genome.bucm.edu.cn/lancelet/index.php) and obtained the consensus sequences of B. floridae ACP3 (bfACP3, with gene ID of 102545) and B. floridae ACP5 (bfACP5, with gene ID of 95439).…”

Section: Cloning Of B Floridae Acp3 Acp5 Myd88 and Traf6mentioning

confidence: 99%

“…We previously identified 21 ACP gene models from the genome and transcriptomes of the amphioxus Branchiostoma floridae (bf) (2). In this study, we cloned the full-length cDNA sequences for bfACP3 and bfACP5, which encode a 561aa protein and a 636aa protein, respectively (Supplementary Figures 1 and 2).…”

Section: Cloning and Sequence Analysis Of Amphioxus Acp3 And Acp5mentioning

confidence: 99%

“…The apextrin C-terminal (ApeC) is a new class of protein domains, characterized by a sequence of about 200 amino acid residues, comprising eight conserved Cysteine residues and three relatively conserved DXED motifs (1). Collectively, here we refer to the proteins containing ApeC domains as ACP (ApeC-containing protein) (2). Comparative genomic analyses show that ACPs exhibit diverse architectures and are widely distributed in many invertebrates.…”

Section: Introductionmentioning

confidence: 99%

“…However, there is no ACPs found in vertebrates and in major arthropod lineages (e.g. insects and crustaceans) except arachnids (2). Distant ApeC homologs were also found in bacteria, hence the origin of ApeC could be traced back to the prokaryotes.…”

Section: Introductionmentioning

confidence: 99%

“…Amphioxus (cephalochordate) is a marine chordate invertebrate, which represents the basal living chordate lineage and is therefore considered as an important proxy to study the evolution from invertebrates to vertebrates (14)(15)(16)(17)(18)(19). Amphioxus has more than twenty ACP genes, hence it can be served as a valuable model to understand the functions and evolution of ACPs (2). In this study, we characterized another two ACPs (bfACP3 and bfACP5) from another amphioxus species (Branchiostoma floridae), which provides a new line of mechanistic evidence for the immune functions of ACPs.…”

Section: Introductionmentioning

confidence: 99%

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Two Amphioxus ApeC-Containing Proteins Bind to Microbes and Inhibit the TRAF6 Pathway

Fan

et al. 2021

Front. Immunol.

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The apextrin C-terminal (ApeC) domain is a class of newly discovered protein domains with an origin dating back to prokaryotes. ApeC-containing proteins (ACPs) have been found in various marine and aquatic invertebrates, but their functions and the underlying mechanisms are largely unknown. Early studies suggested that amphioxus ACP1 and ACP2 bind to bacterial cell walls and have a role in immunity. Here we identified another two amphioxus ACPs (ACP3 and ACP5), which belong to the same phylogenetic clade with ACP1/2, but show distinct expression patterns and sequence divergence (40-50% sequence identities). Both ACP3 and ACP5 were mainly expressed in the intestine and hepatic cecum, and could be up-regulated after bacterial challenge. Both prokaryotic-expressed recombinant ACP3 and ACP5 could bind with several species of bacteria and yeasts, showing agglutinating activity but no microbicidal activity. ELISA assays suggested that their ApeC domains could interact with peptidoglycan (PGN), but not with lipoteichoic acid (LTA), lipopolysaccharides (LPS) and zymosan A. Furthermore, they can only bind to Lys-type PGN from Staphylococcus aureus, but not to DAP-type PGN from Bacillus subtilis and not to moieties of PGN such as MDPs, NAMs and NAGs. This recognition spectrum is different from that of ACP1/2. We also found that when expressed in mammalian cells, ACP3 could interact with TRAF6 via a conserved non-ApeC region, which inhibited the ubiquitination of TRAF6 and hence suppressed downstream NF-κB activation. This work helped define a novel subfamily of ACPs, which have conserved structures, and have related yet diversified molecular functions. Its members have dual roles, with ApeC as a lectin and a conserved unknown region as a signal transduction regulator. These findings expand our understanding of the ACP functions and may guide future research on the role of ACPs in different animal clades.

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Section: Cloning Of B Floridae Acp3 Acp5 Myd88 and Traf6mentioning

confidence: 99%

Section: Cloning and Sequence Analysis Of Amphioxus Acp3 And Acp5mentioning

confidence: 99%