# Cloning and characterization of the LvCTL genes encoding C-type lectin from white-leg shrimp ( Litopenaeus vannamei)

## TL;DR

This paper studies two C-type lectin genes in white-leg shrimp, analyzing their structure and properties to aid future research on their biological functions.

## Contribution

The paper provides new insights into the cloning and characterization of LvCTL3 and LvCTL4 genes in Litopenaeus vannamei.

## Key findings

- LvCTL3 gene is 444 nucleotides long with high similarity to a published gene (KF156943).
- LvCTL4 gene has 417 nucleotides and 100% similarity to a reference polypeptide sequence (AKA64754).
- Both LvCTL3 and LvCTL4 contain one C-type lectin domain with distinct structural features.

## Abstract

Background: Lectins are carbohydrate-binding protein domains. The C-type designates a requirement for calcium for binding. Proteins contain C-type lectin domains that have a diverse range of functions, including cell-cell adhesion, immune response to pathogens, and apoptosis. This study aimed to investigate the characters of LvCTL-encoding genes from white-leg shrimp (
Litopenaeus vannamei) in Central Vietnam.

Methods: Two PCR products (LvCTL3 and LvCTL4) were cloned and sequenced. The structure and characterization of LvCTL proteins were predicted using bioinformatics tools.

Results: The results showed that the
LvCTL
3 gene was 444 nucleotides long and 98.87% similar to the published
LvCTL3 gene (accession number: KF156943). The polypeptide sequence had 147 amino acids, which were 97.28% identical to the reference sequence (AGV68681) and the
LvCT
L4 gene had a length of 417 nucleotides and homology of 99.52% compared to the published gene (KM387560). The deduced polypeptide sequence had 138 amino acids, and was 100% similar to the reference sequence (AKA64754). The
LvCT
L3 had a molecular weight of 16.91 kDa and an isoelectric point (pI) of 4.66, while
LvCTL
4 had 15.75 and 4.58 kDa, respectively. The structure prediction results showed that
LvCTL3 and
LvCTL
4 had one domain (CTLD),
LvCTL
3 had two α helices and nine β sheets, and
LvCTL
4 had two α helices and eight β sheets.

Conclusions: Our results provide essential information for the heterologous expression and biosynthesis production of C-type lectins.