Expression and Characterization of <i>Manduca sexta</i> Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis

Lynn Goss Schrag; Xiaolong Cao; Hawa Dembele; Xiaorong Liu; Qasim Al Souhail; Michael Robert Kanost; Jianhan Chen; Haobo Jiang; Om Prakash

doi:doi:10.11648/j.bmb.20190403.12

Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis

Lynn Goss Schrag, Xiaolong Cao, Hawa Dembele, Xiaorong Liu, Qasim Al Souhail, Michael Robert Kanost, Jianhan Chen, Haobo Jiang, Om Prakash

Published in Biochemistry and Molecular Biology (Volume 4, Issue 3)

Received: 5 July 2019 Accepted: 1 August 2019 Published: 14 August 2019

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Abstract

In response to stress conditions such as wounding or infections in insects, several short peptides are processed to act as cytokines that induce AMP gene expression. To study their structure-activity relationship, immune inducibility, tissue specificity, stress responsiveness, and development relatedness, we chemically synthesized Manduca sexta stress response peptide-1, a 25-residue peptide with one disulfide bond (SRP1: FGVRVGTCPSGYVRRGTFCFPDDDY). Upon injection of the SRP1 into naïve larvae, several antimicrobial peptide genes were expressed at higher levels. The mRNA levels of SRP1 increased significantly in hemocytes and fat body after larvae were challenged with a mixture of bacteria and β-1,3-glucan. The expression patterns of SRP1 and its target genes are somewhat different from SRP2’s, suggesting overlapping yet distinct functions. We elucidated the 3D structure of SRP1 in solution by two-dimensional 1H-1H NMR spectroscopy. The tertiary structure of SRP1 consists of two short β-strands at Y12−R15 and F18−F20, one type-II β-turn at R15−F18 in its well-defined core and is stabilized by a covalent disulfide bond between C8 and C19. The conformational ensemble of SRP1 from extensive atomistic simulation in explicit solvent (with 3.0μs total effective sampling) shows high consistency with experimental intramolecular NOEs of the core region. The SRP1 core adopts a fold similar to the carboxyl-terminal subdomain of epidermal growth factor (EGF), suggesting that SRP1 may interact with EGF receptor-like molecules to trigger its biological function.

Published in	Biochemistry and Molecular Biology (Volume 4, Issue 3)
DOI	10.11648/j.bmb.20190403.12
Page(s)	42-52
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2019. Published by Science Publishing Group

Keywords

Cytokine, Nuclear Magnetic Resonance, Molecular Dynamics, Epidermal Growth Factor, Hemolymph Protein, Insect Immunity, Phenoloxidase

References

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APA Style

Lynn Goss Schrag, Xiaolong Cao, Hawa Dembele, Xiaorong Liu, Qasim Al Souhail, et al. (2019). Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis. Biochemistry and Molecular Biology, 4(3), 42-52. https://doi.org/10.11648/j.bmb.20190403.12

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ACS Style

Lynn Goss Schrag; Xiaolong Cao; Hawa Dembele; Xiaorong Liu; Qasim Al Souhail, et al. Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis. Biochem. Mol. Biol. 2019, 4(3), 42-52. doi: 10.11648/j.bmb.20190403.12

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AMA Style

Lynn Goss Schrag, Xiaolong Cao, Hawa Dembele, Xiaorong Liu, Qasim Al Souhail, et al. Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis. Biochem Mol Biol. 2019;4(3):42-52. doi: 10.11648/j.bmb.20190403.12

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@article{10.11648/j.bmb.20190403.12,
  author = {Lynn Goss Schrag and Xiaolong Cao and Hawa Dembele and Xiaorong Liu and Qasim Al Souhail and Michael Robert Kanost and Jianhan Chen and Haobo Jiang and Om Prakash},
  title = {Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis},
  journal = {Biochemistry and Molecular Biology},
  volume = {4},
  number = {3},
  pages = {42-52},
  doi = {10.11648/j.bmb.20190403.12},
  url = {https://doi.org/10.11648/j.bmb.20190403.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20190403.12},
  abstract = {In response to stress conditions such as wounding or infections in insects, several short peptides are processed to act as cytokines that induce AMP gene expression. To study their structure-activity relationship, immune inducibility, tissue specificity, stress responsiveness, and development relatedness, we chemically synthesized Manduca sexta stress response peptide-1, a 25-residue peptide with one disulfide bond (SRP1: FGVRVGTCPSGYVRRGTFCFPDDDY). Upon injection of the SRP1 into naïve larvae, several antimicrobial peptide genes were expressed at higher levels. The mRNA levels of SRP1 increased significantly in hemocytes and fat body after larvae were challenged with a mixture of bacteria and β-1,3-glucan. The expression patterns of SRP1 and its target genes are somewhat different from SRP2’s, suggesting overlapping yet distinct functions. We elucidated the 3D structure of SRP1 in solution by two-dimensional 1H-1H NMR spectroscopy. The tertiary structure of SRP1 consists of two short β-strands at Y12−R15 and F18−F20, one type-II β-turn at R15−F18 in its well-defined core and is stabilized by a covalent disulfide bond between C8 and C19. The conformational ensemble of SRP1 from extensive atomistic simulation in explicit solvent (with 3.0μs total effective sampling) shows high consistency with experimental intramolecular NOEs of the core region. The SRP1 core adopts a fold similar to the carboxyl-terminal subdomain of epidermal growth factor (EGF), suggesting that SRP1 may interact with EGF receptor-like molecules to trigger its biological function.},
 year = {2019}
}

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TY  - JOUR
T1  - Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis
AU  - Lynn Goss Schrag
AU  - Xiaolong Cao
AU  - Hawa Dembele
AU  - Xiaorong Liu
AU  - Qasim Al Souhail
AU  - Michael Robert Kanost
AU  - Jianhan Chen
AU  - Haobo Jiang
AU  - Om Prakash
Y1  - 2019/08/14
PY  - 2019
N1  - https://doi.org/10.11648/j.bmb.20190403.12
DO  - 10.11648/j.bmb.20190403.12
T2  - Biochemistry and Molecular Biology
JF  - Biochemistry and Molecular Biology
JO  - Biochemistry and Molecular Biology
SP  - 42
EP  - 52
PB  - Science Publishing Group
SN  - 2575-5048
UR  - https://doi.org/10.11648/j.bmb.20190403.12
AB  - In response to stress conditions such as wounding or infections in insects, several short peptides are processed to act as cytokines that induce AMP gene expression. To study their structure-activity relationship, immune inducibility, tissue specificity, stress responsiveness, and development relatedness, we chemically synthesized Manduca sexta stress response peptide-1, a 25-residue peptide with one disulfide bond (SRP1: FGVRVGTCPSGYVRRGTFCFPDDDY). Upon injection of the SRP1 into naïve larvae, several antimicrobial peptide genes were expressed at higher levels. The mRNA levels of SRP1 increased significantly in hemocytes and fat body after larvae were challenged with a mixture of bacteria and β-1,3-glucan. The expression patterns of SRP1 and its target genes are somewhat different from SRP2’s, suggesting overlapping yet distinct functions. We elucidated the 3D structure of SRP1 in solution by two-dimensional 1H-1H NMR spectroscopy. The tertiary structure of SRP1 consists of two short β-strands at Y12−R15 and F18−F20, one type-II β-turn at R15−F18 in its well-defined core and is stabilized by a covalent disulfide bond between C8 and C19. The conformational ensemble of SRP1 from extensive atomistic simulation in explicit solvent (with 3.0μs total effective sampling) shows high consistency with experimental intramolecular NOEs of the core region. The SRP1 core adopts a fold similar to the carboxyl-terminal subdomain of epidermal growth factor (EGF), suggesting that SRP1 may interact with EGF receptor-like molecules to trigger its biological function.
VL  - 4
IS  - 3
ER  -

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Author Information

Lynn Goss Schrag

Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA
Xiaolong Cao

Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, USA
Hawa Dembele

Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA
Xiaorong Liu

Department of Chemistry, University of Massachusetts, Amherst, USA
Qasim Al Souhail

Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA
Michael Robert Kanost

Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA
Jianhan Chen

Department of Chemistry, University of Massachusetts, Amherst, USA
Haobo Jiang

Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, USA
Om Prakash

Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA

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APA Style

Lynn Goss Schrag, Xiaolong Cao, Hawa Dembele, Xiaorong Liu, Qasim Al Souhail, et al. (2019). Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis. Biochemistry and Molecular Biology, 4(3), 42-52. https://doi.org/10.11648/j.bmb.20190403.12

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ACS Style

Lynn Goss Schrag; Xiaolong Cao; Hawa Dembele; Xiaorong Liu; Qasim Al Souhail, et al. Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis. Biochem. Mol. Biol. 2019, 4(3), 42-52. doi: 10.11648/j.bmb.20190403.12

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AMA Style

Lynn Goss Schrag, Xiaolong Cao, Hawa Dembele, Xiaorong Liu, Qasim Al Souhail, et al. Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis. Biochem Mol Biol. 2019;4(3):42-52. doi: 10.11648/j.bmb.20190403.12

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@article{10.11648/j.bmb.20190403.12,
  author = {Lynn Goss Schrag and Xiaolong Cao and Hawa Dembele and Xiaorong Liu and Qasim Al Souhail and Michael Robert Kanost and Jianhan Chen and Haobo Jiang and Om Prakash},
  title = {Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis},
  journal = {Biochemistry and Molecular Biology},
  volume = {4},
  number = {3},
  pages = {42-52},
  doi = {10.11648/j.bmb.20190403.12},
  url = {https://doi.org/10.11648/j.bmb.20190403.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20190403.12},
  abstract = {In response to stress conditions such as wounding or infections in insects, several short peptides are processed to act as cytokines that induce AMP gene expression. To study their structure-activity relationship, immune inducibility, tissue specificity, stress responsiveness, and development relatedness, we chemically synthesized Manduca sexta stress response peptide-1, a 25-residue peptide with one disulfide bond (SRP1: FGVRVGTCPSGYVRRGTFCFPDDDY). Upon injection of the SRP1 into naïve larvae, several antimicrobial peptide genes were expressed at higher levels. The mRNA levels of SRP1 increased significantly in hemocytes and fat body after larvae were challenged with a mixture of bacteria and β-1,3-glucan. The expression patterns of SRP1 and its target genes are somewhat different from SRP2’s, suggesting overlapping yet distinct functions. We elucidated the 3D structure of SRP1 in solution by two-dimensional 1H-1H NMR spectroscopy. The tertiary structure of SRP1 consists of two short β-strands at Y12−R15 and F18−F20, one type-II β-turn at R15−F18 in its well-defined core and is stabilized by a covalent disulfide bond between C8 and C19. The conformational ensemble of SRP1 from extensive atomistic simulation in explicit solvent (with 3.0μs total effective sampling) shows high consistency with experimental intramolecular NOEs of the core region. The SRP1 core adopts a fold similar to the carboxyl-terminal subdomain of epidermal growth factor (EGF), suggesting that SRP1 may interact with EGF receptor-like molecules to trigger its biological function.},
 year = {2019}
}

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TY  - JOUR
T1  - Expression and Characterization of Manduca sexta Stress Responsive Peptide-1; An Inducer of Antimicrobial Peptide Synthesis
AU  - Lynn Goss Schrag
AU  - Xiaolong Cao
AU  - Hawa Dembele
AU  - Xiaorong Liu
AU  - Qasim Al Souhail
AU  - Michael Robert Kanost
AU  - Jianhan Chen
AU  - Haobo Jiang
AU  - Om Prakash
Y1  - 2019/08/14
PY  - 2019
N1  - https://doi.org/10.11648/j.bmb.20190403.12
DO  - 10.11648/j.bmb.20190403.12
T2  - Biochemistry and Molecular Biology
JF  - Biochemistry and Molecular Biology
JO  - Biochemistry and Molecular Biology
SP  - 42
EP  - 52
PB  - Science Publishing Group
SN  - 2575-5048
UR  - https://doi.org/10.11648/j.bmb.20190403.12
AB  - In response to stress conditions such as wounding or infections in insects, several short peptides are processed to act as cytokines that induce AMP gene expression. To study their structure-activity relationship, immune inducibility, tissue specificity, stress responsiveness, and development relatedness, we chemically synthesized Manduca sexta stress response peptide-1, a 25-residue peptide with one disulfide bond (SRP1: FGVRVGTCPSGYVRRGTFCFPDDDY). Upon injection of the SRP1 into naïve larvae, several antimicrobial peptide genes were expressed at higher levels. The mRNA levels of SRP1 increased significantly in hemocytes and fat body after larvae were challenged with a mixture of bacteria and β-1,3-glucan. The expression patterns of SRP1 and its target genes are somewhat different from SRP2’s, suggesting overlapping yet distinct functions. We elucidated the 3D structure of SRP1 in solution by two-dimensional 1H-1H NMR spectroscopy. The tertiary structure of SRP1 consists of two short β-strands at Y12−R15 and F18−F20, one type-II β-turn at R15−F18 in its well-defined core and is stabilized by a covalent disulfide bond between C8 and C19. The conformational ensemble of SRP1 from extensive atomistic simulation in explicit solvent (with 3.0μs total effective sampling) shows high consistency with experimental intramolecular NOEs of the core region. The SRP1 core adopts a fold similar to the carboxyl-terminal subdomain of epidermal growth factor (EGF), suggesting that SRP1 may interact with EGF receptor-like molecules to trigger its biological function.
VL  - 4
IS  - 3
ER  -

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