Sharma, Shailza and Mahajan, Sonal and Sunsunwal, Sonali and Khairnar, Aasawari and Ramya, T N C (2020) Amino acid residues important for D-galactose recognition by the F-type lectin, Ranaspumin-4. Biochemical and biophysical research communications, 532 (1). pp. 54-59. ISSN 0006-291X
Full text not available from this repository. (Request a copy)Abstract
F-type lectins are typically L-fucose binding proteins with characteristic L-fucose-binding and calciumbinding sequence motifs, and an F-type lectin fold. An exception is Ranaspumin-4, an F-type lectin of the Tungra frog, Engystomops pustulosus. Ranaspumin-4 is D-galactose specific and does not bind to L-fucose although it has the conserved L-fucose binding sequence motif and shares overall sequence similarity with other F-type lectins. Here, we report the detailed glycan-binding profile of wild-type Ranaspumin-4 using hemagglutination inhibition assays, flow cytometry assays and enzyme-linked lectin assays, and identify residues important for D-galactose recognition using rational site-directed mutagenesis. We demonstrate that Ranaspumin-4 binds to terminal D-galactose in alpha or beta linkage with preference for alpha 1-3, alpha 1-4,beta 1-3, and beta 1-4 linkages. Further, we find that a methionine residue (M31) in Ranaspumin-4 that occurs in place of a conserved Gln residue (in other F-type lectins), supports D-galactose recognition. Resides Q42 and F156 also likely aid in D-galactose recognition. (C) 2020 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Elsevier Science. |
| Uncontrolled Keywords: | F-type lectin domain; L-fucose; D-galactose; Ranaspumin-4; Site-directed mutagenesis |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 29 Oct 2020 05:33 |
| Last Modified: | 29 Oct 2020 05:33 |
| URI: | http://crdd.osdd.net/open/id/eprint/2611 |
Actions (login required)
 |
View Item |
