Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins.
Bauhinia variegata lectins (BVL-I and BVL-II) are single chain lectins isolated from the plant Bauhinia variegata. Single chain lectins undergo post-translational processing on its N-terminal and C-terminal regions, which determines their physiological targeting, carbohydrate binding activity and pa...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3834338?pdf=render |
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| author | Gustavo M S G Moreira Fabricio R Conceição Alan J A McBride Luciano da S Pinto |
| author_facet | Gustavo M S G Moreira Fabricio R Conceição Alan J A McBride Luciano da S Pinto |
| author_sort | Gustavo M S G Moreira |
| collection | DOAJ |
| description | Bauhinia variegata lectins (BVL-I and BVL-II) are single chain lectins isolated from the plant Bauhinia variegata. Single chain lectins undergo post-translational processing on its N-terminal and C-terminal regions, which determines their physiological targeting, carbohydrate binding activity and pattern of quaternary association. These two lectins are isoforms, BVL-I being highly glycosylated, and thus far, it has not been possible to determine their structures. The present study used prediction and validation algorithms to elucidate the likely structures of BVL-I and -II. The program Bhageerath-H was chosen from among three different structure prediction programs due to its better overall reliability. In order to predict the C-terminal region cleavage sites, other lectins known to have this modification were analysed and three rules were created: (1) the first amino acid of the excised peptide is small or hydrophobic; (2) the cleavage occurs after an acid, polar, or hydrophobic residue, but not after a basic one; and (3) the cleavage spot is located 5-8 residues after a conserved Leu amino acid. These rules predicted that BVL-I and -II would have fifteen C-terminal residues cleaved, and this was confirmed experimentally by Edman degradation sequencing of BVL-I. Furthermore, the C-terminal analyses predicted that only BVL-II underwent α-helical folding in this region, similar to that seen in SBA and DBL. Conversely, BVL-I and -II contained four conserved regions of a GS-I association, providing evidence of a previously undescribed X4+unusual oligomerisation between the truncated BVL-I and the intact BVL-II. This is the first report on the structural analysis of lectins from Bauhinia spp. and therefore is important for the characterisation C-terminal cleavage and patterns of quaternary association of single chain lectins. |
| first_indexed | 2024-12-17T15:16:31Z |
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| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T15:16:31Z |
| publishDate | 2013-01-01 |
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| series | PLoS ONE |
| spelling | doaj.art-e3b05f0870e34fca8011f5cd14b0853f2022-12-21T21:43:32ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-01811e8133810.1371/journal.pone.0081338Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins.Gustavo M S G MoreiraFabricio R ConceiçãoAlan J A McBrideLuciano da S PintoBauhinia variegata lectins (BVL-I and BVL-II) are single chain lectins isolated from the plant Bauhinia variegata. Single chain lectins undergo post-translational processing on its N-terminal and C-terminal regions, which determines their physiological targeting, carbohydrate binding activity and pattern of quaternary association. These two lectins are isoforms, BVL-I being highly glycosylated, and thus far, it has not been possible to determine their structures. The present study used prediction and validation algorithms to elucidate the likely structures of BVL-I and -II. The program Bhageerath-H was chosen from among three different structure prediction programs due to its better overall reliability. In order to predict the C-terminal region cleavage sites, other lectins known to have this modification were analysed and three rules were created: (1) the first amino acid of the excised peptide is small or hydrophobic; (2) the cleavage occurs after an acid, polar, or hydrophobic residue, but not after a basic one; and (3) the cleavage spot is located 5-8 residues after a conserved Leu amino acid. These rules predicted that BVL-I and -II would have fifteen C-terminal residues cleaved, and this was confirmed experimentally by Edman degradation sequencing of BVL-I. Furthermore, the C-terminal analyses predicted that only BVL-II underwent α-helical folding in this region, similar to that seen in SBA and DBL. Conversely, BVL-I and -II contained four conserved regions of a GS-I association, providing evidence of a previously undescribed X4+unusual oligomerisation between the truncated BVL-I and the intact BVL-II. This is the first report on the structural analysis of lectins from Bauhinia spp. and therefore is important for the characterisation C-terminal cleavage and patterns of quaternary association of single chain lectins.http://europepmc.org/articles/PMC3834338?pdf=render |
| spellingShingle | Gustavo M S G Moreira Fabricio R Conceição Alan J A McBride Luciano da S Pinto Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins. PLoS ONE |
| title | Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins. |
| title_full | Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins. |
| title_fullStr | Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins. |
| title_full_unstemmed | Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins. |
| title_short | Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins. |
| title_sort | structure predictions of two bauhinia variegata lectins reveal patterns of c terminal properties in single chain legume lectins |
| url | http://europepmc.org/articles/PMC3834338?pdf=render |
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