2024/06/12 by Keisuke Shimizu, Lumi Negishi, Hitoshi Kurumizaka +1 · 8 citations
Agricultural and Biological Sciences · Environmental Science · Immunology and Microbiology · #Aquaculture Nutrition and Growth #Biochemistry #Biology #Chitin #Diversification (marketing strategy) #Evolutionary biology #Immunology #Invertebrate Immune Response Mechanisms #Parasite Biology and Host Interactions #Platelet #Von Willebrand factor #Zoology
paper · pdf · doi:10.1007/s00239-024-10180-1
published in Journal of Molecular Evolution 92(4), 415-431 (Springer Science+Business Media)
openalex publication_date 2024/06/12 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/06
Pif is a shell matrix protein (SMP) identified in the nacreous layer of Pinctada fucata (Pfu) comprised two proteins, Pif97 and Pif 80. Pif97 contains a von Willebrand factor A (VWA) and chitin-binding domains, whereas Pif80 can bind calcium carbonate crystals. The VWA domain is conserved in the SMPs of various mollusk species; however, their phylogenetic relationship remains obscure. Furthermore, although the VWA domain participates in protein-protein interactions, its role in shell formation has not been established. Accordingly, in the current study, we investigate the phylogenetic relationship between PfuPif and other VWA domain-containing proteins in major mollusk species. The shell-related proteins containing VWA domains formed a large clade (the Pif/BMSP family) and were classified into eight subfamilies with unique sequential features, expression patterns, and taxa diversity. Furthermore, a pull-down assay using recombinant proteins containing the VWA domain of PfuPif 97 revealed that the VWA domain interacts with five nacreous layer-related SMPs of P. fucata, including Pif 80 and nacrein. Collectively, these results suggest that the VWA domain is important in the formation of organic complexes and participates in shell mineralisation.