A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union

Rajesh K. Grover; Xueyong Zhu; Travis Nieusma; Teresa Jones; Isabel Boero; Amanda S. MacLeod; Adam Mark; Sherry Niessen; Helen J. Kim; Leopold Kong; Nacyra Assad-Garcia; Keehwan Kwon; Marta Chesi; Vaughn V. Smider; Daniel R. Salomon; Diane F. Jelinek; Robert A. Kyle; Richard B. Pyles; John I. Glass; Andrew B. Ward; Ian A. Wilson; Richard A. Lerner

doi:10.1126/science.1246135

A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union

Rajesh K. Grover, Xueyong Zhu, Travis Nieusma, Teresa Jones, Isabel Boero, Amanda S. MacLeod, Adam Mark, Sherry Niessen, Helen J. Kim, Leopold Kong, Nacyra Assad-Garcia, Keehwan Kwon, Marta Chesi, Vaughn V. Smider, Daniel R. Salomon, Diane F. Jelinek, Robert A. Kyle, Richard B. Pyles, John I. Glass, Andrew B. WardIan A. Wilson, Richard A. Lerner

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

48 Scopus citations

Abstract

We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the k and l light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field.

Original language	English (US)
Pages (from-to)	656-661
Number of pages	6
Journal	Science
Volume	343
Issue number	6171
DOIs	https://doi.org/10.1126/science.1246135
State	Published - 2014
Externally published	Yes

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Grover, R. K., Zhu, X., Nieusma, T., Jones, T., Boero, I., MacLeod, A. S., Mark, A., Niessen, S., Kim, H. J., Kong, L., Assad-Garcia, N., Kwon, K., Chesi, M., Smider, V. V., Salomon, D. R., Jelinek, D. F., Kyle, R. A., Pyles, R. B., Glass, J. I., ... Lerner, R. A. (2014). A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. Science, 343(6171), 656-661. https://doi.org/10.1126/science.1246135

Grover, RK, Zhu, X, Nieusma, T, Jones, T, Boero, I, MacLeod, AS, Mark, A, Niessen, S, Kim, HJ, Kong, L, Assad-Garcia, N, Kwon, K, Chesi, M, Smider, VV, Salomon, DR, Jelinek, DF, Kyle, RA, Pyles, RB, Glass, JI, Ward, AB, Wilson, IA & Lerner, RA 2014, 'A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union', Science, vol. 343, no. 6171, pp. 656-661. https://doi.org/10.1126/science.1246135

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title = "A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union",

abstract = "We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the k and l light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field.",

author = "Grover, {Rajesh K.} and Xueyong Zhu and Travis Nieusma and Teresa Jones and Isabel Boero and MacLeod, {Amanda S.} and Adam Mark and Sherry Niessen and Kim, {Helen J.} and Leopold Kong and Nacyra Assad-Garcia and Keehwan Kwon and Marta Chesi and Smider, {Vaughn V.} and Salomon, {Daniel R.} and Jelinek, {Diane F.} and Kyle, {Robert A.} and Pyles, {Richard B.} and Glass, {John I.} and Ward, {Andrew B.} and Wilson, {Ian A.} and Lerner, {Richard A.}",

year = "2014",

doi = "10.1126/science.1246135",

language = "English (US)",

volume = "343",

pages = "656--661",

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AU - Grover, Rajesh K.

AU - Zhu, Xueyong

AU - Nieusma, Travis

AU - Jones, Teresa

AU - Boero, Isabel

AU - MacLeod, Amanda S.

AU - Mark, Adam

AU - Niessen, Sherry

AU - Kim, Helen J.

AU - Kong, Leopold

AU - Assad-Garcia, Nacyra

AU - Kwon, Keehwan

AU - Chesi, Marta

AU - Smider, Vaughn V.

AU - Salomon, Daniel R.

AU - Jelinek, Diane F.

AU - Kyle, Robert A.

AU - Pyles, Richard B.

AU - Glass, John I.

AU - Ward, Andrew B.

AU - Wilson, Ian A.

AU - Lerner, Richard A.

PY - 2014

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AB - We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the k and l light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field.

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A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union

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