Fish Physiology and Biochemistry

, Volume 39, Issue 6, pp 1619–1630

Domain composition of rhamnose-binding lectin from shishamo smelt eggs and its carbohydrate-binding profiles

  • Masahiro Hosono
  • Shigeki Sugawara
  • Takeo Tatsuta
  • Toshiyuki Hikita
  • Junko Kominami
  • Sachiko Nakamura-Tsuruta
  • Jun Hirabayashi
  • Sarkar M. A. Kawsar
  • Yasuhiro Ozeki
  • Sen-itiroh Hakomori
  • Kazuo Nitta
Article

DOI: 10.1007/s10695-013-9814-6

Cite this article as:
Hosono, M., Sugawara, S., Tatsuta, T. et al. Fish Physiol Biochem (2013) 39: 1619. doi:10.1007/s10695-013-9814-6
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Abstract

Osmerus (Spirinchus) lanceolatus egg lectin (OLL) is a member of the rhamnose-binding lectin (RBL) family which is mainly found in aqueous beings. cDNA of OLL was cloned, and its genomic architecture was revealed. The deduced amino acid (aa) sequence indicated that OLL was composed of 213 aa including 95 aa of domain N and 97 aa of domain C. N and C showed 73 % sequence identity and contained both -ANYGR- and -DPC-KYL-peptide motifs which are conserved in most of the RBL carbohydrate recognition domains. The calculated molecular mass of mature OLL was 20,852, consistent with the result, and 20,677.716, from mass spectrometry. OLL was encoded by eight exons: exons 1 and 2 for a signal peptide; exons 3–5 and 6–8 for N- and C-domains, respectively. Surface plasmon resonance spectrometric analyses revealed that OLL showed comparable affinity for Galα- and β-linkages, whereas Silurus asotus lectin (SAL), a catfish RBL, bound preferentially to α-linkages of neoglycoproteins. The Kd values of OLL and SAL against globotriaosylceramide (Gb3) were 1.69 × 10−5 M for and 2.81 × 10−6 M, respectively. Thus, the carbohydrate recognition property of OLL is slightly different from that of SAL. On the other hand, frontal affinity chromatography revealed that both OLL and SAL interacted with only glycolipid-type oligosaccharides such as Gb3 trisaccharides, not with N-linked oligosaccharides. The domain composition of these RBLs and an analytical environment such as the “cluster effect” of a ligand might influence the binding between RBL and sugar chains.

Keywords

Lectin Fish eggs Domain structure Carbohydrate-binding Rhamnose 

Abbreviations

RBL

Rhamnose-binding lectin

OLL

Osmerus lanceolatus lectin

SAL

Silurus asotus lectin

SPR

Surface plasmon resonance

FAC

Frontal affinity chromatography

CRD

Carbohydrate recognition domain

Supplementary material

10695_2013_9814_MOESM1_ESM.doc (33 kb)
Supplementary material 1 (DOC 33 kb)

Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Masahiro Hosono
    • 1
  • Shigeki Sugawara
    • 1
  • Takeo Tatsuta
    • 1
  • Toshiyuki Hikita
    • 2
  • Junko Kominami
    • 3
  • Sachiko Nakamura-Tsuruta
    • 3
  • Jun Hirabayashi
    • 4
  • Sarkar M. A. Kawsar
    • 5
  • Yasuhiro Ozeki
    • 6
  • Sen-itiroh Hakomori
    • 7
    • 8
  • Kazuo Nitta
    • 1
  1. 1.Division of Cell Recognition Study, Institute of Molecular Biomembrane and GlycobiologyTohoku Pharmaceutical UniversitySendaiJapan
  2. 2.Department of PediatricsTeikyo University School of MedicineTokyoJapan
  3. 3.Research Center for Medical GlycosciencesNational Institute of Advanced Industrial Science and TechnologyTsukubaJapan
  4. 4.Research Center for Stem Cell EngineeringNational Institute of Advanced Industrial Science and TechnologyTsukubaJapan
  5. 5.Laboratory of Carbohydrate and Protein Chemistry, Department of Chemistry, Faculty of ScienceUniversity of ChittagongChittagongBangladesh
  6. 6.Laboratory of Glycobiology and Marine Biochemistry, Department of Life and Environmental System Science, Graduate School of NanoBio SciencesYokohama City UniversityYokohamaJapan
  7. 7.Division of Biomembrane ResearchPacific Northwest Research InstituteSeattleUSA
  8. 8.Departments of Pathobiology and MicrobiologyUniversity of WashingtonSeattleUSA

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