Purification and partial characterization of carbohydrate-recognition protein C-type lectin from Hemifusus pugilinus

Jeyachandran Sivakamavalli; Kiyun Park; Ihn-Sil Kwak; Baskaralingam Vaseeharan

doi:10.1016/j.carres.2020.108224

Purification and partial characterization of carbohydrate-recognition protein C-type lectin from Hemifusus pugilinus

Carbohydr Res. 2021 Jan:499:108224. doi: 10.1016/j.carres.2020.108224. Epub 2020 Dec 30.

Authors

Jeyachandran Sivakamavalli¹, Kiyun Park², Ihn-Sil Kwak³, Baskaralingam Vaseeharan⁴

Affiliations

¹ Fisheries Science Institute, Chonnam National University, Yeosu, 59626, South Korea; Department of Biotechnology & Microbiology, National College, Tiruchirappalli, 620001, India; Department of Animal Health and Management, Alagappa University, Karaikudi, 630 003, Tamil Nadu, India. Electronic address: dr.jsvalli@gmail.com.
² Fisheries Science Institute, Chonnam National University, Yeosu, 59626, South Korea; Department of Biotechnology & Microbiology, National College, Tiruchirappalli, 620001, India. Electronic address: ecoblue@hotmail.com.
³ Fisheries Science Institute, Chonnam National University, Yeosu, 59626, South Korea; Department of Biotechnology & Microbiology, National College, Tiruchirappalli, 620001, India; Faculty of Marine Technology, Chonnam National University, Yeosu, 59626, South Korea. Electronic address: inkwak@hotmail.com.
⁴ Department of Animal Health and Management, Alagappa University, Karaikudi, 630 003, Tamil Nadu, India. Electronic address: vaseeharanb@gmail.com.

PMID: 33450477
DOI: 10.1016/j.carres.2020.108224

Abstract

A mannose binding lectin (C-type lectin) was detected in a molluscan snail Hemifusus pugilinus, this lectin molecule was isolated and purified from the plasma using mannose-fixed sepharose CL-4B column affinity chromatography. The purified protein corresponds to the molecular weight of 118 kDa on an SDS-PAGE gel. The divalent cation-dependent nature of the H. pugilinus lectin (Hp-Lec) evidenced through pH and thermal stability analysis using Circular Dichroism (CD) and Surface Plasmon Resonance (SPR) respectively. Functional investigations of the Hp-Lec reveal a broad spectrum of bacterial agglutination activity against wide range of Gram-positive and Gram-negative bacterial strains. Furthermore, Hp-Lec displayed the haemo agglutination activity against vertebrate red blood cells (RBCs) and its titers were recorded. Excitingly, microbial virulent pathogens such as fungal strains tested against the purified Hp-Lec (25 and 50 μg/ml), which exhibits the effective antifungal activity against tested fungal pathogens such as Aspergillus niger and A. flavus.

Keywords: A. flavus; A. niger; Agglutination activity; Bacterial agglutination; H. pugilinus, lectin.

MeSH terms

Animals
Carbohydrate Conformation
Carbohydrates / chemistry*
Gastropoda / chemistry*
Lectins, C-Type / chemistry
Lectins, C-Type / isolation & purification*

Substances

Carbohydrates
Lectins, C-Type