Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/13925
ชื่อเรื่อง: Therapeutic epitopes of Leptospira LipL32 protein and their characteristics
ผู้แต่ง: Maneewatch S.
Adisakwattana P.
Chaisri U.
Saengjaruk P.
Srimanote P.
Thanongsaksrikul J.
Sakolvaree Y.
Poungpan P.
Chaicumpa W.
Keywords: Amino acids
Cell adhesion
Monoclonal antibodies
Proteins
Adhesive matrices
Epitope mapping
Leptospirosis
Mimotopes
Neutralizing mAb
Epitopes
amino acid
epitope
leptospirosis vaccine
neutralizing antibody
outer membrane protein LipL32
phospholipid
epitope
LipL32 protein, Leptospira
lipoprotein
monoclonal antibody
neutralizing antibody
outer membrane protein
amino acid sequence
article
cell adhesion
enzyme linked immunosorbent assay
hemolysis
in vitro study
Leptospira
leptospirosis
nonhuman
priority journal
animal
antibody specificity
chemical structure
chemistry
epitope mapping
hamster
immunology
Leptospira
leptospirosis
molecular genetics
mouse
physiology
protein secondary structure
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antibodies, Neutralizing
Antibody Specificity
Bacterial Outer Membrane Proteins
Cricetinae
Epitope Mapping
Epitopes
Leptospira
Leptospirosis
Lipoproteins
Mice
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary
วันที่เผยแพร่: 2014
บทคัดย่อ: Two LipL32-specific mouse monoclonal antibodies (mAbLPF1 and mAbLPF2) which neutralized Leptospira-mediated hemolysis in vitro and rescued hamsters from lethal Leptospira infection were produced. In this communication, locations and characteristics of the protective epitopes of the mAbs were studied by using a truncated LipL32 recombinant protein based-immunoassay and phage consensus mimotope identification and multiple alignments. The mAbLPF1 epitope consisted of P243, L244, I245, H246, L252 and Q253 on the LipL32 protein; it is mapped on the surface-exposed region of non-continuous β13-turn and C-terminal amphipathic α6 helix with hydrophobic patch, contributing to phospholipid/host cell adhesion and membrane insertion on one side, and hydrophilic, acidic and basic amino acid residues on another side. The epitope peptide of the mAbLPF2 is linear 122PEEKSMPHW130 and located on surface-exposed α1 and α2 between β7 and β8 that bound to several host constituents. Both epitopes are highly conserved among the pathogenic and intermediately pathogenic Leptospira spp. and are absent from the LipL32 superfamily proteins of other microorganisms. This study not only enlightens the molecular mechanisms of the therapeutic mAbLPF1 and mAbLPF2, but also elaborates the potential of the two LipL32 regions as diagnostic and vaccine targets for leptospirosis. © 2014 The Author. Published by Oxford University Press. All rights reserved.
URI: https://ir.swu.ac.th/jspui/handle/123456789/13925
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84899844581&doi=10.1093%2fprotein%2fgzu006&partnerID=40&md5=40fa30e3f23ea91df8c7460dbb1bba7c
ISSN: 17410126
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.


Items in SWU repository are protected by copyright, with all rights reserved, unless otherwise indicated.