Abstract
The glycobiology of the cestodes, a class of parasitic flatworms, is still largely unexplored. An important cestode species is Echinococcus granulosus, the tissue-dwelling larval stage of which causes hydatid disease. The E. granulosus larva is protected from the host by a massive mucin-based extracellular matrix termed laminated layer (LL). We previously reported (Díaz et al. 2009. Biochemistry 48:11678-11691) the molecular structure of the most abundant LL O-glycans, comprising up to six monosaccharide residues. These are based on Cores 1 and 2, in cases elongated by a chain of Galpß1-3 residues, which can be capped by Galpß1-4. In addition, the Core 2 GlcNAcp residue can be decorated with the Galpß1-4Galpß1-4 disaccharide. Larger glycans also detected contained additional HexNAc residues that could not be explained by the structural repertoire described above. In this work, we elucidate, by mass spectrometry (MS) and nuclear magnetic resonance (NMR), six additional glycans from the E. granulosus LL between six and eight residues in size. Their structures are related to those already described but in cases bear GlcNAcpß1-6 or Galpß1-4Galpß1-4GlcNAcpß1-6 as ramifications on the core Galpß1-3 residue. We also obtained evidence that noncore Galpß1-3 residues can be similarly ramified. Thus, the new motif together with the previous information may explain all the glycan compositions detected in the LL by MS. In addition, we show that the anti-Echinococcus monoclonal antibody E492 (Parasite Immunol 21:141, 1999) recognizes Galpß1-4Galpß1-4GlcNAcp (the blood P1-antigen motif). This explains the antibody's reactivity with a range of Echinococcus tissues, as the P1-motif is also carried on non-LL N-glycans and glycolipids from this genus.
| Original language | English |
|---|---|
| Pages (from-to) | 438-452 |
| Number of pages | 15 |
| Journal | Glycobiology |
| Volume | 23 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2013 Apr |
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Keywords
- cestode
- Echinococcus
- mucin
- O-glycan
- P-blood group antigen
ASJC Scopus subject areas
- Biochemistry
Cite this
Further structural characterization of the Echinococcus granulosus laminated layer carbohydrates : The blood-antigen P1-motif gives rise to branches at different points of the O-glycan chains. / Lin, Gerardo; Todeschini, Adriane R.; Koizumi, Akihiko; Neves, Jorge L.; González, Humberto; Dematteis, Sylvia; Hada, Noriyasu; Previato, Jose O.; Ferreira, Fernando; Mendonça-Previato, Lucia; Díaz, Alvaro.
In: Glycobiology, Vol. 23, No. 4, 04.2013, p. 438-452.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Further structural characterization of the Echinococcus granulosus laminated layer carbohydrates
T2 - The blood-antigen P1-motif gives rise to branches at different points of the O-glycan chains
AU - Lin, Gerardo
AU - Todeschini, Adriane R.
AU - Koizumi, Akihiko
AU - Neves, Jorge L.
AU - González, Humberto
AU - Dematteis, Sylvia
AU - Hada, Noriyasu
AU - Previato, Jose O.
AU - Ferreira, Fernando
AU - Mendonça-Previato, Lucia
AU - Díaz, Alvaro
PY - 2013/4
Y1 - 2013/4
N2 - The glycobiology of the cestodes, a class of parasitic flatworms, is still largely unexplored. An important cestode species is Echinococcus granulosus, the tissue-dwelling larval stage of which causes hydatid disease. The E. granulosus larva is protected from the host by a massive mucin-based extracellular matrix termed laminated layer (LL). We previously reported (Díaz et al. 2009. Biochemistry 48:11678-11691) the molecular structure of the most abundant LL O-glycans, comprising up to six monosaccharide residues. These are based on Cores 1 and 2, in cases elongated by a chain of Galpß1-3 residues, which can be capped by Galpß1-4. In addition, the Core 2 GlcNAcp residue can be decorated with the Galpß1-4Galpß1-4 disaccharide. Larger glycans also detected contained additional HexNAc residues that could not be explained by the structural repertoire described above. In this work, we elucidate, by mass spectrometry (MS) and nuclear magnetic resonance (NMR), six additional glycans from the E. granulosus LL between six and eight residues in size. Their structures are related to those already described but in cases bear GlcNAcpß1-6 or Galpß1-4Galpß1-4GlcNAcpß1-6 as ramifications on the core Galpß1-3 residue. We also obtained evidence that noncore Galpß1-3 residues can be similarly ramified. Thus, the new motif together with the previous information may explain all the glycan compositions detected in the LL by MS. In addition, we show that the anti-Echinococcus monoclonal antibody E492 (Parasite Immunol 21:141, 1999) recognizes Galpß1-4Galpß1-4GlcNAcp (the blood P1-antigen motif). This explains the antibody's reactivity with a range of Echinococcus tissues, as the P1-motif is also carried on non-LL N-glycans and glycolipids from this genus.
AB - The glycobiology of the cestodes, a class of parasitic flatworms, is still largely unexplored. An important cestode species is Echinococcus granulosus, the tissue-dwelling larval stage of which causes hydatid disease. The E. granulosus larva is protected from the host by a massive mucin-based extracellular matrix termed laminated layer (LL). We previously reported (Díaz et al. 2009. Biochemistry 48:11678-11691) the molecular structure of the most abundant LL O-glycans, comprising up to six monosaccharide residues. These are based on Cores 1 and 2, in cases elongated by a chain of Galpß1-3 residues, which can be capped by Galpß1-4. In addition, the Core 2 GlcNAcp residue can be decorated with the Galpß1-4Galpß1-4 disaccharide. Larger glycans also detected contained additional HexNAc residues that could not be explained by the structural repertoire described above. In this work, we elucidate, by mass spectrometry (MS) and nuclear magnetic resonance (NMR), six additional glycans from the E. granulosus LL between six and eight residues in size. Their structures are related to those already described but in cases bear GlcNAcpß1-6 or Galpß1-4Galpß1-4GlcNAcpß1-6 as ramifications on the core Galpß1-3 residue. We also obtained evidence that noncore Galpß1-3 residues can be similarly ramified. Thus, the new motif together with the previous information may explain all the glycan compositions detected in the LL by MS. In addition, we show that the anti-Echinococcus monoclonal antibody E492 (Parasite Immunol 21:141, 1999) recognizes Galpß1-4Galpß1-4GlcNAcp (the blood P1-antigen motif). This explains the antibody's reactivity with a range of Echinococcus tissues, as the P1-motif is also carried on non-LL N-glycans and glycolipids from this genus.
KW - cestode
KW - Echinococcus
KW - mucin
KW - O-glycan
KW - P-blood group antigen
UR - http://www.scopus.com/inward/record.url?scp=84874690460&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84874690460&partnerID=8YFLogxK
U2 - 10.1093/glycob/cws220
DO - 10.1093/glycob/cws220
M3 - Article
C2 - 23263200
AN - SCOPUS:84874690460
VL - 23
SP - 438
EP - 452
JO - Glycobiology
JF - Glycobiology
SN - 0959-6658
IS - 4
ER -