Publication:
Therapeutic epitopes of Leptospira LipL32 protein and their characteristics

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Issued Date

2014

Resource Type

Article

File Type

application/pdf

ISSN

17410126

DOI

10.1093/protein/gzu006

Other identifier(s)

2-s2.0-84899844581

Rights Holder(s)

Scopus

Bibliographic Citation

Protein Engineering, Design and Selection. Vol 27, No.5 (2014), p.135-144

Suggested Citation

Maneewatch S., Adisakwattana P., Chaisri U., Saengjaruk P., Srimanote P., Thanongsaksrikul J., Sakolvaree Y., Poungpan P., Chaicumpa W. Therapeutic epitopes of Leptospira LipL32 protein and their characteristics. Protein Engineering, Design and Selection. Vol 27, No.5 (2014), p.135-144. doi:10.1093/protein/gzu006 Retrieved from: https://hdl.handle.net/20.500.14740/6452

Title

Therapeutic epitopes of Leptospira LipL32 protein and their characteristics

Author(s)

Maneewatch S.
 Adisakwattana P.
 Chaisri U.
 Saengjaruk P.
 Srimanote P.
 Thanongsaksrikul J.
 Sakolvaree Y.
 Poungpan P.
 Chaicumpa W.

Abstract

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.

Subject(s)

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

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URI

https://hdl.handle.net/20.500.14740/6452

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Scopus: Year 1983-2021

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