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\begin{document}

\title{Structural and allergenic properties of the Fatty Acid Binding Protein
from shrimp \emph{Litopenaeus vannamei}}



\author[1]{Marlon Munera}%
\author[2]{Dalgys Martinez}%
\author[3]{Judith Wortmann}%
\author[1]{Josefina Zakzuk}%
\author[3]{Walter Keller}%
\author[1]{Luis Caraballo}%
\author[4]{Leonardo Puerta}%
\affil[1]{University of Cartagena}%
\affil[2]{University of Cartagena Institute of Immunological Research}%
\affil[3]{University of Graz}%
\affil[4]{Universidad de Cartagena}%


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  \date{May 15, 2024}


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\begin{abstract}
Background: The shrimp \emph{Litopaneus vanammei} is an important source
of food allergens but its allergenic repertoire is poorly characterized.
Cross reactivity between crustacean and mites has been characterized,
with tropomyosin, the most relevant allergen involved. The aim of this
study was the structural and immunological characterization of an
allergen belonging to the Fatty Acid Binding Protein (FABP) family from
L. vannamei (LvFABP). Methods: ELISA, skin prick test (SPT) and basophil
activation assays were performed to determine IgE reactivity and
allergenicity of LvFABP. LC-MS/MS and Circular Dichroism experiments
were done for structural analysis. B-cell epitope mapping with
overlapping peptides, and cross-inhibition studies using human sera were
done to identify antigenic regions and cross-reactivity. Results: The
recombinant LvFABP showed IgE reactivity in 27\% of allergic patients
tested and showed allergenic activity when tested for basophil
activation and SPT in shrimp sensitized patients. CD-spectroscopy of
LvFABP revealed that the protein is folded with a secondary structure
composed of mainly \selectlanguage{greek}β-\selectlanguage{english}strands and a smaller fraction of ? helices. This
is consistent with molecular modelling results, which exhibit a typical
\selectlanguage{greek}β \selectlanguage{english}barrel fold with two \selectlanguage{greek}α-\selectlanguage{english}helices and ten \selectlanguage{greek}β-\selectlanguage{english}strands. Epitope mapping
identified two IgE binding antigenic regions and inhibition assays found
high cross reactivity between LvFABP and Blo t 13, mediated by the
antigenic region involving amino acids 53 to 73. Conclusions: Our
results support LvFABP as an allergen with cross reactivity with the
allergen Blo t 13. This new allergen could help to understand new
mechanisms of sensitization to seafood such as shrimp.%
\end{abstract}%



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