Crystal structure of the receptor-binding domain of botulinum neurotoxin type HA, also known as type FA or H
Abstract
Botulinum neurotoxins (BoNTs), which have been exploited as cosmetics and muscle-disorder treatment medicines for decades, are well known for their extreme neurotoxicity to humans. They pose a potential bioterrorism threat because they cause botulism, a flaccid muscular paralysis-associated disease that requires immediate antitoxin treatment and intensive care over a long period of time. In addition to the existing seven established BoNT serotypes (BoNT/A–G), a new mosaic toxin type termed BoNT/HA (aka type FA or H) was reported recently. Sequence analyses indicate that the receptor-binding domain (HC) of BoNT/HA is ~84% identical to that of BoNT/A1. However, BoNT/HA responds differently to some potent BoNT/A-neutralizing antibodies (e.g., CR2) that target the HC. Therefore, it raises a serious concern as to whether BoNT/HA poses a new threat to our biosecurity. In this study, we report the first high-resolution crystal structure of BoNT/HA-HC at 1.8 Å. Sequence and structure analyses reveal that BoNT/HA and BoNT/A1 are different regarding their binding to cell-surface receptors including both polysialoganglioside (PSG) and synaptic vesicle glycoprotein 2 (SV2). Furthermore, the new structure also provides explanations for the ~540-fold decreased affinity of antibody CR2 towards BoNT/HA compared to BoNT/A1. Altogether, these new findings advance our understanding of the structure andmore »
- Authors:
-
[3];
- Univ. of California, Irvine, CA (United States)
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Medizinische Hochschule Hannover, Hannover (Germany)
- Publication Date:
- Research Org.:
- Univ. of California, Irvine, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1355928
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Toxins
- Additional Journal Information:
- Journal Volume: 9; Journal Issue: 3; Journal ID: ISSN 2072-6651
- Publisher:
- MDPI
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES; 59 BASIC BIOLOGICAL SCIENCES; botulinum neurotoxin (BoNT); BoNT/HA; BoNT/H; BoNT/FA; receptor-binding domain; host receptor; neutralizing antibody
Citation Formats
Yao, Guorui, Lam, Kwok-ho, Perry, Kay, Weisemann, Jasmin, Rummel, Andreas, and Jin, Rongsheng. Crystal structure of the receptor-binding domain of botulinum neurotoxin type HA, also known as type FA or H. United States: N. p., 2017.
Web. doi:10.3390/toxins9030093.
Yao, Guorui, Lam, Kwok-ho, Perry, Kay, Weisemann, Jasmin, Rummel, Andreas, & Jin, Rongsheng. Crystal structure of the receptor-binding domain of botulinum neurotoxin type HA, also known as type FA or H. United States. https://doi.org/10.3390/toxins9030093
Yao, Guorui, Lam, Kwok-ho, Perry, Kay, Weisemann, Jasmin, Rummel, Andreas, and Jin, Rongsheng. Wed .
"Crystal structure of the receptor-binding domain of botulinum neurotoxin type HA, also known as type FA or H". United States. https://doi.org/10.3390/toxins9030093. https://www.osti.gov/servlets/purl/1355928.
@article{osti_1355928,
title = {Crystal structure of the receptor-binding domain of botulinum neurotoxin type HA, also known as type FA or H},
author = {Yao, Guorui and Lam, Kwok-ho and Perry, Kay and Weisemann, Jasmin and Rummel, Andreas and Jin, Rongsheng},
abstractNote = {Botulinum neurotoxins (BoNTs), which have been exploited as cosmetics and muscle-disorder treatment medicines for decades, are well known for their extreme neurotoxicity to humans. They pose a potential bioterrorism threat because they cause botulism, a flaccid muscular paralysis-associated disease that requires immediate antitoxin treatment and intensive care over a long period of time. In addition to the existing seven established BoNT serotypes (BoNT/A–G), a new mosaic toxin type termed BoNT/HA (aka type FA or H) was reported recently. Sequence analyses indicate that the receptor-binding domain (HC) of BoNT/HA is ~84% identical to that of BoNT/A1. However, BoNT/HA responds differently to some potent BoNT/A-neutralizing antibodies (e.g., CR2) that target the HC. Therefore, it raises a serious concern as to whether BoNT/HA poses a new threat to our biosecurity. In this study, we report the first high-resolution crystal structure of BoNT/HA-HC at 1.8 Å. Sequence and structure analyses reveal that BoNT/HA and BoNT/A1 are different regarding their binding to cell-surface receptors including both polysialoganglioside (PSG) and synaptic vesicle glycoprotein 2 (SV2). Furthermore, the new structure also provides explanations for the ~540-fold decreased affinity of antibody CR2 towards BoNT/HA compared to BoNT/A1. Altogether, these new findings advance our understanding of the structure and function of this newly identified toxin at the molecular level, and pave the way for the future development of more effective countermeasures.},
doi = {10.3390/toxins9030093},
journal = {Toxins},
number = 3,
volume = 9,
place = {United States},
year = {Wed Mar 08 00:00:00 EST 2017},
month = {Wed Mar 08 00:00:00 EST 2017}
}
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