Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae

Ju Ho Youn; Han Jeong Myung; Abraham Liav; Delphi Chatterjee; Patrick J. Brennan; In Hong Choi; Sang Nae Cho; Jeon Soo Shin

doi:10.1016/j.femsim.2004.01.001

Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae

Ju Ho Youn, Han Jeong Myung, Abraham Liav, Delphi Chatterjee, Patrick J. Brennan, In Hong Choi, Sang Nae Cho, Jeon Soo Shin

Department of Microbiology

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

Phenolic glycolipid-I (PGL-I), a Mycobacterium leprae-specific antigen, has been widely used for the serodiagnosis of leprosy and has been implicated in the pathogenesis of leprosy. In an effort to produce an alternate antigen of PGL-I, the mimotope peptides of PGL-I, W(T/R)LGPY(V/M), were obtained using a monoclonal antibody, III603.8, specific to PGL-I by a phage library. The biotin-labeled predominant mimotope peptide of PGLP1, WTLGPYV, bound to III603.8 in a dose-dependent manner in an immunoassay. However, PGLP1 did not bind to anti-PGL-I antibodies in the serum samples from leprosy patients that were reactive to PGL-I. Although the mimotope peptide of WTLGPYV was not effective as an alternate antigen of PGL-I for the serodiagnosis of leprosy, but it would be of interest to know how the mimotope peptides mimic the role of PGL-I antigen in the pathogenesis of M. leprae infection.

Original language	English
Pages (from-to)	51-57
Number of pages	7
Journal	FEMS Immunology and Medical Microbiology
Volume	41
Issue number	1
DOIs	https://doi.org/10.1016/j.femsim.2004.01.001
Publication status	Published - 2004 May 1

Bibliographical note

Funding Information:
The work was supported by a grant from The Heiser Program of The New York Community Trust, by a grant from the National Research Laboratory Program (M1-0204-00-0146), of the Ministry of Science and Technology National Research and Development Program, Korea, and by grant from National Institutes of Health (AI47197), USA. The PGL-I and its related antigens and neoglycoconjugates were provided via the contract NO1 AI55262 from the National Institute of Allergy and Infectious Diseases, National Institutes of Health, USA.

All Science Journal Classification (ASJC) codes

Immunology and Allergy
Microbiology
Immunology
Microbiology (medical)
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.femsim.2004.01.001

Cite this

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title = "Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae",

abstract = "Phenolic glycolipid-I (PGL-I), a Mycobacterium leprae-specific antigen, has been widely used for the serodiagnosis of leprosy and has been implicated in the pathogenesis of leprosy. In an effort to produce an alternate antigen of PGL-I, the mimotope peptides of PGL-I, W(T/R)LGPY(V/M), were obtained using a monoclonal antibody, III603.8, specific to PGL-I by a phage library. The biotin-labeled predominant mimotope peptide of PGLP1, WTLGPYV, bound to III603.8 in a dose-dependent manner in an immunoassay. However, PGLP1 did not bind to anti-PGL-I antibodies in the serum samples from leprosy patients that were reactive to PGL-I. Although the mimotope peptide of WTLGPYV was not effective as an alternate antigen of PGL-I for the serodiagnosis of leprosy, but it would be of interest to know how the mimotope peptides mimic the role of PGL-I antigen in the pathogenesis of M. leprae infection.",

author = "Youn, {Ju Ho} and Myung, {Han Jeong} and Abraham Liav and Delphi Chatterjee and Brennan, {Patrick J.} and Choi, {In Hong} and Cho, {Sang Nae} and Shin, {Jeon Soo}",

note = "Funding Information: The work was supported by a grant from The Heiser Program of The New York Community Trust, by a grant from the National Research Laboratory Program (M1-0204-00-0146), of the Ministry of Science and Technology National Research and Development Program, Korea, and by grant from National Institutes of Health (AI47197), USA. The PGL-I and its related antigens and neoglycoconjugates were provided via the contract NO1 AI55262 from the National Institute of Allergy and Infectious Diseases, National Institutes of Health, USA.",

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doi = "10.1016/j.femsim.2004.01.001",

language = "English",

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AU - Youn, Ju Ho

AU - Myung, Han Jeong

AU - Liav, Abraham

AU - Chatterjee, Delphi

AU - Brennan, Patrick J.

AU - Choi, In Hong

AU - Cho, Sang Nae

AU - Shin, Jeon Soo

N1 - Funding Information: The work was supported by a grant from The Heiser Program of The New York Community Trust, by a grant from the National Research Laboratory Program (M1-0204-00-0146), of the Ministry of Science and Technology National Research and Development Program, Korea, and by grant from National Institutes of Health (AI47197), USA. The PGL-I and its related antigens and neoglycoconjugates were provided via the contract NO1 AI55262 from the National Institute of Allergy and Infectious Diseases, National Institutes of Health, USA.

PY - 2004/5/1

Y1 - 2004/5/1

N2 - Phenolic glycolipid-I (PGL-I), a Mycobacterium leprae-specific antigen, has been widely used for the serodiagnosis of leprosy and has been implicated in the pathogenesis of leprosy. In an effort to produce an alternate antigen of PGL-I, the mimotope peptides of PGL-I, W(T/R)LGPY(V/M), were obtained using a monoclonal antibody, III603.8, specific to PGL-I by a phage library. The biotin-labeled predominant mimotope peptide of PGLP1, WTLGPYV, bound to III603.8 in a dose-dependent manner in an immunoassay. However, PGLP1 did not bind to anti-PGL-I antibodies in the serum samples from leprosy patients that were reactive to PGL-I. Although the mimotope peptide of WTLGPYV was not effective as an alternate antigen of PGL-I for the serodiagnosis of leprosy, but it would be of interest to know how the mimotope peptides mimic the role of PGL-I antigen in the pathogenesis of M. leprae infection.

AB - Phenolic glycolipid-I (PGL-I), a Mycobacterium leprae-specific antigen, has been widely used for the serodiagnosis of leprosy and has been implicated in the pathogenesis of leprosy. In an effort to produce an alternate antigen of PGL-I, the mimotope peptides of PGL-I, W(T/R)LGPY(V/M), were obtained using a monoclonal antibody, III603.8, specific to PGL-I by a phage library. The biotin-labeled predominant mimotope peptide of PGLP1, WTLGPYV, bound to III603.8 in a dose-dependent manner in an immunoassay. However, PGLP1 did not bind to anti-PGL-I antibodies in the serum samples from leprosy patients that were reactive to PGL-I. Although the mimotope peptide of WTLGPYV was not effective as an alternate antigen of PGL-I for the serodiagnosis of leprosy, but it would be of interest to know how the mimotope peptides mimic the role of PGL-I antigen in the pathogenesis of M. leprae infection.

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Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

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