Abstract
Owing to the weak reactivities of monomeric dManα1 and Galβ1→3/4GlcNAcβ (Iβ/IIβ) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes lFucα1→, dManα1→ and Iβ/IIβ within two combining sites were established by both enzyme-linked lectinosorbent and inhibition assays. It was found that high density of lFucα1→ complex enhanced the recognition intensities at lFucα1→ site, polyvalent dManα1→ was essential for binding at the dManα1→ site and polyvalent I β/IIβ was required at lFucα1→ site. The peculiar recognition systems of RSL are very different from other well known microbial lectins.
Original language | English |
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Pages (from-to) | 1294-1299 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 586 |
Issue number | 9 |
DOIs | |
State | Published - 7 May 2012 |
Bibliographical note
Funding Information:This work was supported by Grants from the Chang-Gung Medical Research Project (CMRP No. 180482 and 170443), Kwei-san, Tao-yuan, Taiwan, the National Science Council (NSC 100-2320-B-182-027 and 100-2320-B-182-028), Taipei, Taiwan. The authors thank for Ms. Yu Ping Gong’s technical assistance and data collection.
Funding
This work was supported by Grants from the Chang-Gung Medical Research Project (CMRP No. 180482 and 170443), Kwei-san, Tao-yuan, Taiwan, the National Science Council (NSC 100-2320-B-182-027 and 100-2320-B-182-028), Taipei, Taiwan. The authors thank for Ms. Yu Ping Gong’s technical assistance and data collection.
Funders | Funder number |
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CMRP | 170443, 180482 |
Chang-Gung Medical Research Project | |
National Science Council | 100-2320-B-182-028, 100-2320-B-182-027 |
Keywords
- ABH active O-glycans
- Carbohydrate recognition domain
- Mannan
- Ralstonia solanacearum lectin