Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins
Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of <i>Pteria penguin</i> (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PP...
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doaj-805c6943f85447cdb3debebd38048cb02021-01-23T00:02:53ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-01-01221081108110.3390/ijms22031081Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix ProteinsTomohisa Ogawa0Rie Sato1Takako Naganuma2Kayeu Liu3Saho Sato4Shizuka Sakaue5Makoto Osada6Kyosuke Yoshimi7Koji Muramoto8Graduate School of Agricultural Science, Tohoku University, Sendai 980-8572, JapanGraduate School of Life Sciences, Tohoku University, Sendai 980-8577, JapanGraduate School of Life Sciences, Tohoku University, Sendai 980-8577, JapanGraduate School of Life Sciences, Tohoku University, Sendai 980-8577, JapanGraduate School of Life Sciences, Tohoku University, Sendai 980-8577, JapanGraduate School of Life Sciences, Tohoku University, Sendai 980-8577, JapanGraduate School of Agricultural Science, Tohoku University, Sendai 980-8572, JapanCenter for Interdisciplinary Research, Tohoku University, Sendai 980-8578, JapanGraduate School of Life Sciences, Tohoku University, Sendai 980-8577, JapanPreviously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of <i>Pteria penguin</i> (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO<sub>3</sub> crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO<sub>3</sub> calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO<sub>3</sub> crystalization; however, PPL4 regulated the size of crystals collaborated with <i>N</i>-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation.https://www.mdpi.com/1422-0067/22/3/1081biomineralizationcarbohydratechitinlectinpearl shell |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Tomohisa Ogawa Rie Sato Takako Naganuma Kayeu Liu Saho Sato Shizuka Sakaue Makoto Osada Kyosuke Yoshimi Koji Muramoto |
spellingShingle |
Tomohisa Ogawa Rie Sato Takako Naganuma Kayeu Liu Saho Sato Shizuka Sakaue Makoto Osada Kyosuke Yoshimi Koji Muramoto Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins International Journal of Molecular Sciences biomineralization carbohydrate chitin lectin pearl shell |
author_facet |
Tomohisa Ogawa Rie Sato Takako Naganuma Kayeu Liu Saho Sato Shizuka Sakaue Makoto Osada Kyosuke Yoshimi Koji Muramoto |
author_sort |
Tomohisa Ogawa |
title |
Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins |
title_short |
Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins |
title_full |
Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins |
title_fullStr |
Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins |
title_full_unstemmed |
Diversified Biomineralization Roles of <i>Pteria penguin</i> Pearl Shell Lectins as Matrix Proteins |
title_sort |
diversified biomineralization roles of <i>pteria penguin</i> pearl shell lectins as matrix proteins |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-01-01 |
description |
Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of <i>Pteria penguin</i> (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO<sub>3</sub> crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO<sub>3</sub> calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO<sub>3</sub> crystalization; however, PPL4 regulated the size of crystals collaborated with <i>N</i>-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation. |
topic |
biomineralization carbohydrate chitin lectin pearl shell |
url |
https://www.mdpi.com/1422-0067/22/3/1081 |
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