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.

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.

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