Heterologous expression and mutagenesis of recombinant Vespa affinis hyaluronidase protein (rVesA2)

Crude venom of the banded tiger wasp contains a variety of enzymes including hyaluronidases, commonly known as spreading factors. The cDNA cloning, sequence analysis and structural modelling of venom hyaluronidase (VesA2) were herein described. Moreover, heterologous expression and mutagenesis of rV...

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Published inThe journal of venomous animals and toxins including tropical diseases Vol. 25; p. e20190030
Main Authors Rungsa, Prapenpuksiri, Janpan, Piyapon, Saengkun, Yutthakan, Jangpromma, Nisachon, Klaynongsruang, Sompong, Patramanon, Rina, Uawonggul, Nunthawun, Daduang, Jureerut, Daduang, Sakda
Format Journal Article
LanguageEnglish
Portuguese
Published Brazil Centro de Estudos de Venenos e Animais Peçonhentos 2019
Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
SciELO
Subjects
Cloning
Hyaluronidase
Modelling
Protein expression
Structure analysis
TOXICOLOGY
TROPICAL MEDICINE
Vespa affinis
Wasp, Venom
Hyaluronidase
Vespa affinis
Wasp, Venom
Cloning
Protein expression
Modelling
Structure analysis
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Abstract Crude venom of the banded tiger wasp contains a variety of enzymes including hyaluronidases, commonly known as spreading factors. The cDNA cloning, sequence analysis and structural modelling of venom hyaluronidase (VesA2) were herein described. Moreover, heterologous expression and mutagenesis of rVesA2 were performed. venom hyaluronidase full sequence is composed of 331 amino acids, with four predicted -glycosylation sites. It was classified into the glycoside hydrolase family 56. The homology modelling exhibited a central core (α/β) composed of Asp107 and Glu109, acting as the catalytic residues. The recombinant protein was successfully expressed in with hyaluronidase activity. A recombinant mutant type with the double point mutation, Asp107Asn and Glu109Gln, completely lost this activity. The hyaluronidase from crude venom exhibited activity from pH 2 to 7. The recombinant wild type showed its maximal activity at pH 2 but decreased rapidly to nearly zero at pH 3 and was completely lost at pH 4. The recombinant wild-type protein showed its maximal activity at pH 2, more acidic pH than that found in the crude venom. The glycosylation was predicted to be responsible for the pH optimum and thermal stability of the enzymes activity.
AbstractList Abstract Background: Crude venom of the banded tiger waspVespa affinis contains a variety of enzymes including hyaluronidases, commonly known as spreading factors. Methods: The cDNA cloning, sequence analysis and structural modelling of V. affinis venom hyaluronidase (VesA2) were herein described. Moreover, heterologous expression and mutagenesis of rVesA2 were performed. Results: V. affinis venom hyaluronidase full sequence is composed of 331 amino acids, with four predicted N-glycosylation sites. It was classified into the glycoside hydrolase family 56. The homology modelling exhibited a central core (α/β)7 composed of Asp107 and Glu109, acting as the catalytic residues. The recombinant protein was successfully expressed in E. coli with hyaluronidase activity. A recombinant mutant type with the double point mutation, Asp107Asn and Glu109Gln, completely lost this activity. The hyaluronidase from crude venom exhibited activity from pH 2 to 7. The recombinant wild type showed its maximal activity at pH 2 but decreased rapidly to nearly zero at pH 3 and was completely lost at pH 4. Conclusion: The recombinant wild-type protein showed its maximal activity at pH 2, more acidic pH than that found in the crude venom. The glycosylation was predicted to be responsible for the pH optimum and thermal stability of the enzymes activity.
Crude venom of the banded tiger wasp contains a variety of enzymes including hyaluronidases, commonly known as spreading factors. The cDNA cloning, sequence analysis and structural modelling of venom hyaluronidase (VesA2) were herein described. Moreover, heterologous expression and mutagenesis of rVesA2 were performed. venom hyaluronidase full sequence is composed of 331 amino acids, with four predicted -glycosylation sites. It was classified into the glycoside hydrolase family 56. The homology modelling exhibited a central core (α/β) composed of Asp107 and Glu109, acting as the catalytic residues. The recombinant protein was successfully expressed in with hyaluronidase activity. A recombinant mutant type with the double point mutation, Asp107Asn and Glu109Gln, completely lost this activity. The hyaluronidase from crude venom exhibited activity from pH 2 to 7. The recombinant wild type showed its maximal activity at pH 2 but decreased rapidly to nearly zero at pH 3 and was completely lost at pH 4. The recombinant wild-type protein showed its maximal activity at pH 2, more acidic pH than that found in the crude venom. The glycosylation was predicted to be responsible for the pH optimum and thermal stability of the enzymes activity.
Author Klaynongsruang, Sompong
Daduang, Sakda
Daduang, Jureerut
Janpan, Piyapon
Rungsa, Prapenpuksiri
Jangpromma, Nisachon
Uawonggul, Nunthawun
Saengkun, Yutthakan
Patramanon, Rina
AuthorAffiliation 3 Faculty of Science, Nakhon Phanom University, Nakhon Phanom, 48000, Thailand
4 Centre for Research and Development of Medical Diagnostic Laboratories, Faculty of Associated Medical Sciences, Khon Kaen University, Khon Kaen, Thailand
2 Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand
1 Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand
AuthorAffiliation_xml – name: 2 Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand
– name: 4 Centre for Research and Development of Medical Diagnostic Laboratories, Faculty of Associated Medical Sciences, Khon Kaen University, Khon Kaen, Thailand
– name: 1 Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand
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  surname: Rungsa
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  givenname: Piyapon
  surname: Janpan
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  surname: Jangpromma
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  givenname: Rina
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  surname: Patramanon
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– sequence: 7
  givenname: Nunthawun
  surname: Uawonggul
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  organization: Faculty of Science, Nakhon Phanom University, Nakhon Phanom, 48000, Thailand
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  surname: Daduang
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  organization: Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand
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Keywords Hyaluronidase
Vespa affinis
Wasp, Venom
Cloning
Protein expression
Modelling
Structure analysis
Language English
Portuguese
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Notes Authors’ contributions: PR and PJ conducted most of the experiments, coordinated the data analysis and drafted the manuscript. YS carried out partial molecular biology techniques. NJ performed the bioinformatics analysis. SK, RP and NU contributed to the study design and editing manuscript. JD performed the molecular analyses and contributed to the editing of the manuscript. SD designed the research and the experiments, coordinated the study, wrote and edited the manuscript. All authors read and approved the final manuscript.
Competing interests: The authors declare that they have no competing interests.
ORCID 0000-0002-2071-2406
0000-0002-9325-2527
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0000-0003-2672-7710
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PMID 31839801
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PublicationTitle The journal of venomous animals and toxins including tropical diseases
PublicationTitleAlternate J Venom Anim Toxins Incl Trop Dis
PublicationYear 2019
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Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
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SSID ssj0029083
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Snippet Crude venom of the banded tiger wasp contains a variety of enzymes including hyaluronidases, commonly known as spreading factors. The cDNA cloning, sequence...
Abstract Background: Crude venom of the banded tiger waspVespa affinis contains a variety of enzymes including hyaluronidases, commonly known as spreading...
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StartPage e20190030
SubjectTerms Cloning
Hyaluronidase
Modelling
Protein expression
Structure analysis
TOXICOLOGY
TROPICAL MEDICINE
Vespa affinis
Wasp, Venom
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Title Heterologous expression and mutagenesis of recombinant Vespa affinis hyaluronidase protein (rVesA2)
URI https://www.ncbi.nlm.nih.gov/pubmed/31839801
https://pubmed.ncbi.nlm.nih.gov/PMC6892566
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https://doaj.org/article/8e27f3a3196a4c8eb0aea9e70eee7f21
Volume 25
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