Antibody recognition of Shiga toxins (Stxs): Computational identification of the epitopes of Stx2 subunit A to the antibodies 11E10 and S2C4

Yongjun Jiao, Fiona Sue Legge, Xiaoyan Zeng, Herbert Rudulf Treutlein, Jun Zeng

Research output: Contribution to journalArticleResearchpeer-review

3 Citations (Scopus)

Abstract

We have recently developed a new method to predict the epitopes of the antigens that are recognized by a specific antibody. In this work, we applied the method to identify the epitopes of the Shiga toxin (Stx2 subunit A) that were bound by two specific antibodies 11E10 and S2C4. The predicted epitopes of Stx2 binding to the antibody 11E10 resembles the recognition surface constructed by the regions of Stx2 identified experimentally. For the S2C4, our results indicate that the antibody recognizes the Stx2 at two different regions on the protein surface. The first region (residues 246-254: ARSVRAVNE) is similar to the recognition region of the 11E10, while the second region is formed by two epitopes. The second region is particularly significant because it includes the amino acid sequence region that is diverse between Stx2 and other Stx (residues 176-188: QREFRQALSETAPV). This new recognition region is believed to play an important role in the experimentally observed selectivity of S2C4 to the Stx2.
Original languageEnglish
Article numbere88191
Number of pages12
JournalPLoS ONE
Volume9
Issue number2
DOIs
Publication statusPublished - 2014

Cite this

Jiao, Yongjun ; Legge, Fiona Sue ; Zeng, Xiaoyan ; Treutlein, Herbert Rudulf ; Zeng, Jun. / Antibody recognition of Shiga toxins (Stxs): Computational identification of the epitopes of Stx2 subunit A to the antibodies 11E10 and S2C4. In: PLoS ONE. 2014 ; Vol. 9, No. 2.
@article{4ec593cd36cd4e5394f5a6e84e98aed8,
title = "Antibody recognition of Shiga toxins (Stxs): Computational identification of the epitopes of Stx2 subunit A to the antibodies 11E10 and S2C4",
abstract = "We have recently developed a new method to predict the epitopes of the antigens that are recognized by a specific antibody. In this work, we applied the method to identify the epitopes of the Shiga toxin (Stx2 subunit A) that were bound by two specific antibodies 11E10 and S2C4. The predicted epitopes of Stx2 binding to the antibody 11E10 resembles the recognition surface constructed by the regions of Stx2 identified experimentally. For the S2C4, our results indicate that the antibody recognizes the Stx2 at two different regions on the protein surface. The first region (residues 246-254: ARSVRAVNE) is similar to the recognition region of the 11E10, while the second region is formed by two epitopes. The second region is particularly significant because it includes the amino acid sequence region that is diverse between Stx2 and other Stx (residues 176-188: QREFRQALSETAPV). This new recognition region is believed to play an important role in the experimentally observed selectivity of S2C4 to the Stx2.",
author = "Yongjun Jiao and Legge, {Fiona Sue} and Xiaoyan Zeng and Treutlein, {Herbert Rudulf} and Jun Zeng",
year = "2014",
doi = "10.1371/journal.pone.0088191",
language = "English",
volume = "9",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "2",

}

Antibody recognition of Shiga toxins (Stxs): Computational identification of the epitopes of Stx2 subunit A to the antibodies 11E10 and S2C4. / Jiao, Yongjun; Legge, Fiona Sue; Zeng, Xiaoyan; Treutlein, Herbert Rudulf; Zeng, Jun.

In: PLoS ONE, Vol. 9, No. 2, e88191, 2014.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Antibody recognition of Shiga toxins (Stxs): Computational identification of the epitopes of Stx2 subunit A to the antibodies 11E10 and S2C4

AU - Jiao, Yongjun

AU - Legge, Fiona Sue

AU - Zeng, Xiaoyan

AU - Treutlein, Herbert Rudulf

AU - Zeng, Jun

PY - 2014

Y1 - 2014

N2 - We have recently developed a new method to predict the epitopes of the antigens that are recognized by a specific antibody. In this work, we applied the method to identify the epitopes of the Shiga toxin (Stx2 subunit A) that were bound by two specific antibodies 11E10 and S2C4. The predicted epitopes of Stx2 binding to the antibody 11E10 resembles the recognition surface constructed by the regions of Stx2 identified experimentally. For the S2C4, our results indicate that the antibody recognizes the Stx2 at two different regions on the protein surface. The first region (residues 246-254: ARSVRAVNE) is similar to the recognition region of the 11E10, while the second region is formed by two epitopes. The second region is particularly significant because it includes the amino acid sequence region that is diverse between Stx2 and other Stx (residues 176-188: QREFRQALSETAPV). This new recognition region is believed to play an important role in the experimentally observed selectivity of S2C4 to the Stx2.

AB - We have recently developed a new method to predict the epitopes of the antigens that are recognized by a specific antibody. In this work, we applied the method to identify the epitopes of the Shiga toxin (Stx2 subunit A) that were bound by two specific antibodies 11E10 and S2C4. The predicted epitopes of Stx2 binding to the antibody 11E10 resembles the recognition surface constructed by the regions of Stx2 identified experimentally. For the S2C4, our results indicate that the antibody recognizes the Stx2 at two different regions on the protein surface. The first region (residues 246-254: ARSVRAVNE) is similar to the recognition region of the 11E10, while the second region is formed by two epitopes. The second region is particularly significant because it includes the amino acid sequence region that is diverse between Stx2 and other Stx (residues 176-188: QREFRQALSETAPV). This new recognition region is believed to play an important role in the experimentally observed selectivity of S2C4 to the Stx2.

UR - http://www.plosone.org/article/fetchObject.action?uri=info:doi/10.1371/journal.pone.0088191&representation=PDF

U2 - 10.1371/journal.pone.0088191

DO - 10.1371/journal.pone.0088191

M3 - Article

VL - 9

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 2

M1 - e88191

ER -