Proteomics and Immunological Analysis of Arginine Kinase, an Important Shrimp Allergen from Litopenaeus vannamei

doi:10.7506/spkx1002-6630-201501032

Abstract

Abstract:

This study aimed to identify the 40-kD allergen of Litopenaeus vannamei and to analyze its immune crossreactivity
among shellfish species. Several proteomics and immunological experiments were performed. By using matrixassisted
laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF-MS), the 40 kD allergen from
Litopenaeus vannamei was identified as arginine kinase (AK). Its amino acid sequence was compared with that of known
proteins by BLAST, Clustal X2 and MEGA 5. The results revealed that AK had high homology among shrimp (96%－100%),
crab (91%－93%), cockroach (83%) and mollusca (49%－52%)．The purified AK was injected subcutaneously into mice
to produce specific polyclonal antibodies for analyzing its immune cross-reactivity by Western blotting. It was shown that
the proteins with relative molecular mass (Mr) of about 40 kD corresponding to AKs from 17 species of shellfish could be
recognized by the AK-specific polyclonal sera. The results of both proteomics and immunological analysis have shown that
AK is a pan-allergen among crustacean and mollusca.

Key words: Litopenaeus vannamei, allergen, arginine kinase, mass spectrometry, sequence homology, immune cross-reactivity

CLC Number:

R392.8

SUN Yifan, HUANG Jianfang, XIANG Junjian*, WANG Caixia, CHEN Chengfeng. Proteomics and Immunological Analysis of Arginine Kinase, an Important Shrimp Allergen from Litopenaeus vannamei[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201501032.

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Proteomics and Immunological Analysis of Arginine Kinase, an Important Shrimp Allergen from Litopenaeus vannamei

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