Glycan Binding Profiling of Jacalin-Related Lectins from the Pteria Penguin Pearl Shell.

Tomohisa Ogawa,Rie Sato,Koji Muramoto,Kayeu Liu,Takako Naganuma,Kyosuke Yoshimi,Agness Ethel Lakudzala,Jun Hirabayashi,Makoto Osada,Keiko Hiemori,Hiroaki Tateno

doi:10.3390/ijms20184629

Abstract

We determined the primary structures of jacalin-related lectins termed PPL3s (PPL3A, 3B, and 3C, which are dimers consisting of sequence variants α + α, α + β, β + β, respectively) and PPL4, which is heterodimer consisting of α + β subunits, isolated from mantle secretory fluid of Pteria penguin (Mabe) pearl shell. Their carbohydrate-binding properties were analyzed, in addition to that of PPL2A, which was previously reported as a matrix protein. PPL3s and PPL4 shared only 35–50% homology to PPL2A, respectively; they exhibited significantly different carbohydrate-binding specificities based on the multiple glycan binding profiling data sets from frontal affinity chromatography analysis. The carbohydrate-binding specificity of PPL3s was similar to that of PPL2A, except only for Man3Fuc1Xyl1GlcNAc2 oligosaccharide, while PPL4 showed different carbohydrate-binding specificity compared with PPL2A and PPL3s. PPL2A and PPL3s mainly recognize agalactosylated- and galactosylated-type glycans. On the other hand, PPL4 binds to high-mannose-and hybrid-type N-linked glycans but not agalactosylated- and galactosylated-type glycans.

Highlights

Biomineralization is the crystallization process of inorganic materials under strict biological control in nature
The amino acid sequences of PPL3 and PPL4 subunits showed sequence homologies with PPL2A and PPL2B, which were previously isolated from the mantle of Pteria penguin [23]
Multiple sequence alignment of PPL3 and PPL4 subunits with jacalin-related lectin (JRL) revealed that the structural elements for the carbohydrate recognition domain (CRD) were conserved among PPLs and JRLs, including the GG loop (Gly28/Gly31) and the binding loop (Gly149/Asp153) at the top of β-prism fold [30,31,32], PPLs have low sequence identity with other JRLs (Figure 2)

Summary

Introduction

Biomineralization is the crystallization process of inorganic materials under strict biological control in nature. Splice variants of perlucin, of which C-terminal region include repeat sequence, has been identified [19] These diversifications of C-type lectins were observed in the spicule matrix proteins of sea urchin, which include Pro-rich repeat domain and/or acidic repeat domain [20]. We identified and characterized novel matrix proteins, PPL2A and PPL2B, which are dimers composed of α + γ and β + β subunits, respectively, and are homologous to jacalin-related-prism fold lectins, from P. penguin mantle and nacre [23]. We determined the primary structures of two jacalin-related lectins, termed PPL3s and PPL4, which were isolated from the mantle-secreted fluid of P. penguin, and analyzed their carbohydrate-binding properties, in addition to that of PPL2A, in detail

Results

Discussion

Amino Acid Sequences of PPL3 and PPL4 Subunits

Sugar-Binding Specificity