Characterization of a novel binding protein for Fortilin/TCTP - component of a defense mechanism against viral infection in Penaeus monodon

Tanate Panrat, Patuma Sinthujaroen, Benjamas Nupan, Warapond Wanna, Martti Tapani Tammi, Amornrat Phongdara

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca 2+-binding domain at residues 76-110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45-55 and 123-145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the "x-G-K-K" pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the "x-P-P-x" patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin.

Original languageEnglish (US)
Article numbere33291
JournalPLoS One
Volume7
Issue number3
DOIs
StatePublished - Mar 12 2012
Externally publishedYes

Fingerprint

Penaeidae
Penaeus monodon
Virus Diseases
defense mechanisms
binding proteins
Carrier Proteins
infection
White spot syndrome virus 1
White spot syndrome virus
transmembrane proteins
disulfide bonds
Bioinformatics
Computational Biology
Viruses
Protein Binding
bioinformatics
Disulfides
Computer Simulation
Antiviral Agents
binding sites

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Characterization of a novel binding protein for Fortilin/TCTP - component of a defense mechanism against viral infection in Penaeus monodon. / Panrat, Tanate; Sinthujaroen, Patuma; Nupan, Benjamas; Wanna, Warapond; Tammi, Martti Tapani; Phongdara, Amornrat.

In: PLoS One, Vol. 7, No. 3, e33291, 12.03.2012.

Research output: Contribution to journalArticle

Panrat, Tanate ; Sinthujaroen, Patuma ; Nupan, Benjamas ; Wanna, Warapond ; Tammi, Martti Tapani ; Phongdara, Amornrat. / Characterization of a novel binding protein for Fortilin/TCTP - component of a defense mechanism against viral infection in Penaeus monodon. In: PLoS One. 2012 ; Vol. 7, No. 3.
@article{1c1b69a7a4ac4a5baec55d7fed9e80af,
title = "Characterization of a novel binding protein for Fortilin/TCTP - component of a defense mechanism against viral infection in Penaeus monodon",
abstract = "The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca 2+-binding domain at residues 76-110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45-55 and 123-145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the {"}x-G-K-K{"} pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the {"}x-P-P-x{"} patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin.",
author = "Tanate Panrat and Patuma Sinthujaroen and Benjamas Nupan and Warapond Wanna and Tammi, {Martti Tapani} and Amornrat Phongdara",
year = "2012",
month = "3",
day = "12",
doi = "10.1371/journal.pone.0033291",
language = "English (US)",
volume = "7",
journal = "PLoS One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "3",

}

TY - JOUR

T1 - Characterization of a novel binding protein for Fortilin/TCTP - component of a defense mechanism against viral infection in Penaeus monodon

AU - Panrat, Tanate

AU - Sinthujaroen, Patuma

AU - Nupan, Benjamas

AU - Wanna, Warapond

AU - Tammi, Martti Tapani

AU - Phongdara, Amornrat

PY - 2012/3/12

Y1 - 2012/3/12

N2 - The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca 2+-binding domain at residues 76-110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45-55 and 123-145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the "x-G-K-K" pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the "x-P-P-x" patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin.

AB - The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca 2+-binding domain at residues 76-110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45-55 and 123-145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the "x-G-K-K" pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the "x-P-P-x" patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin.

UR - http://www.scopus.com/inward/record.url?scp=84858050284&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84858050284&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0033291

DO - 10.1371/journal.pone.0033291

M3 - Article

VL - 7

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 3

M1 - e33291

ER -