Academic Journal
Self-Assembly of Tail Tube Protein of Bacteriophage vB_EcoS_NBD2 into Extremely Long Polytubes in E. coli and S. cerevisiae
العنوان: | Self-Assembly of Tail Tube Protein of Bacteriophage vB_EcoS_NBD2 into Extremely Long Polytubes in E. coli and S. cerevisiae |
---|---|
المؤلفون: | Aliona Špakova, Eugenijus Šimoliūnas, Raminta Batiuškaitė, Simonas Pajeda, Rolandas Meškys, Rasa Petraitytė-Burneikienė |
المصدر: | Viruses, Vol 11, Iss 3, p 208 (2019) |
بيانات النشر: | MDPI AG, 2019. |
سنة النشر: | 2019 |
المجموعة: | LCC:Microbiology |
مصطلحات موضوعية: | bacteriophage vB_EcoS_NBD2, tail tube protein, self-assembly, tubular structure, polytubes, stability, Saccharomyces cerevisiae, Escherichia coli, Microbiology, QR1-502 |
الوصف: | Nucleotides, peptides and proteins serve as a scaffold material for self-assembling nanostructures. In this study, the production of siphovirus vB_EcoS_NBD2 (NBD2) recombinant tail tube protein gp39 reached approximately 33% and 27% of the total cell protein level in Escherichia coli and Saccharomyces cerevisiae expression systems, respectively. A simple purification protocol allowed us to produce a recombinant gp39 protein with 85%–90% purity. The yield of gp39 was 2.9 ± 0.36 mg/g of wet E. coli cells and 0.85 ± 0.33 mg/g for S. cerevisiae cells. The recombinant gp39 self-assembled into well-ordered tubular structures (polytubes) in vivo in the absence of other phage proteins. The diameter of these structures was the same as the diameter of the tail of phage NBD2 (~12 nm). The length of these structures varied from 0.1 µm to >3.95 µm, which is 23-fold the normal NBD2 tail length. Stability analysis demonstrated that the polytubes could withstand various chemical and physical conditions. These polytubes show the potential to be used as a nanomaterial in various fields of science. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 1999-4915 11030208 |
Relation: | http://www.mdpi.com/1999-4915/11/3/208; https://doaj.org/toc/1999-4915 |
DOI: | 10.3390/v11030208 |
URL الوصول: | https://doaj.org/article/dd9581b8c822443daeb58dae169f4433 |
رقم الانضمام: | edsdoj.9581b8c822443daeb58dae169f4433 |
قاعدة البيانات: | Directory of Open Access Journals |
ResultId |
1 |
---|---|
Header |
edsdoj Directory of Open Access Journals edsdoj.9581b8c822443daeb58dae169f4433 879 3 Academic Journal academicJournal 878.714538574219 |
PLink |
https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&scope=site&db=edsdoj&AN=edsdoj.9581b8c822443daeb58dae169f4433&custid=s6537998&authtype=sso |
FullText |
Array
(
[Availability] => 0
)
Array ( [0] => Array ( [Url] => https://doaj.org/article/dd9581b8c822443daeb58dae169f4433 [Name] => EDS - DOAJ [Category] => fullText [Text] => View record in DOAJ [MouseOverText] => View record in DOAJ ) [1] => Array ( [Url] => https://resolver.ebscohost.com/openurl?custid=s6537998&groupid=main&authtype=ip,guest&sid=EBSCO:edsdoj&genre=article&issn=19994915&ISBN=&volume=11&issue=3&date=20190301&spage=208&pages=208-208&title=Viruses&atitle=Self-Assembly%20of%20Tail%20Tube%20Protein%20of%20Bacteriophage%20vB_EcoS_NBD2%20into%20Extremely%20Long%20Polytubes%20in%20E.%20coli%20and%20S.%20cerevisiae&id=DOI:10.3390/v11030208 [Name] => Full Text Finder (s6537998api) [Category] => fullText [Text] => Full Text Finder [Icon] => https://imageserver.ebscohost.com/branding/images/FTF.gif [MouseOverText] => Full Text Finder ) ) |
Items |
Array
(
[Name] => Title
[Label] => Title
[Group] => Ti
[Data] => Self-Assembly of Tail Tube Protein of Bacteriophage vB_EcoS_NBD2 into Extremely Long Polytubes in E. coli and S. cerevisiae
)
Array ( [Name] => Author [Label] => Authors [Group] => Au [Data] => <searchLink fieldCode="AR" term="%22Aliona+Špakova%22">Aliona Špakova</searchLink><br /><searchLink fieldCode="AR" term="%22Eugenijus+Šimoliūnas%22">Eugenijus Šimoliūnas</searchLink><br /><searchLink fieldCode="AR" term="%22Raminta+Batiuškaitė%22">Raminta Batiuškaitė</searchLink><br /><searchLink fieldCode="AR" term="%22Simonas+Pajeda%22">Simonas Pajeda</searchLink><br /><searchLink fieldCode="AR" term="%22Rolandas+Meškys%22">Rolandas Meškys</searchLink><br /><searchLink fieldCode="AR" term="%22Rasa+Petraitytė-Burneikienė%22">Rasa Petraitytė-Burneikienė</searchLink> ) Array ( [Name] => TitleSource [Label] => Source [Group] => Src [Data] => Viruses, Vol 11, Iss 3, p 208 (2019) ) Array ( [Name] => Publisher [Label] => Publisher Information [Group] => PubInfo [Data] => MDPI AG, 2019. ) Array ( [Name] => DatePubCY [Label] => Publication Year [Group] => Date [Data] => 2019 ) Array ( [Name] => Subset [Label] => Collection [Group] => HoldingsInfo [Data] => LCC:Microbiology ) Array ( [Name] => Subject [Label] => Subject Terms [Group] => Su [Data] => <searchLink fieldCode="DE" term="%22bacteriophage+vB%5FEcoS%5FNBD2%22">bacteriophage vB_EcoS_NBD2</searchLink><br /><searchLink fieldCode="DE" term="%22tail+tube+protein%22">tail tube protein</searchLink><br /><searchLink fieldCode="DE" term="%22self-assembly%22">self-assembly</searchLink><br /><searchLink fieldCode="DE" term="%22tubular+structure%22">tubular structure</searchLink><br /><searchLink fieldCode="DE" term="%22polytubes%22">polytubes</searchLink><br /><searchLink fieldCode="DE" term="%22stability%22">stability</searchLink><br /><searchLink fieldCode="DE" term="%22Saccharomyces+cerevisiae%22">Saccharomyces cerevisiae</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22Microbiology%22">Microbiology</searchLink><br /><searchLink fieldCode="DE" term="%22QR1-502%22">QR1-502</searchLink> ) Array ( [Name] => Abstract [Label] => Description [Group] => Ab [Data] => Nucleotides, peptides and proteins serve as a scaffold material for self-assembling nanostructures. In this study, the production of siphovirus vB_EcoS_NBD2 (NBD2) recombinant tail tube protein gp39 reached approximately 33% and 27% of the total cell protein level in Escherichia coli and Saccharomyces cerevisiae expression systems, respectively. A simple purification protocol allowed us to produce a recombinant gp39 protein with 85%–90% purity. The yield of gp39 was 2.9 ± 0.36 mg/g of wet E. coli cells and 0.85 ± 0.33 mg/g for S. cerevisiae cells. The recombinant gp39 self-assembled into well-ordered tubular structures (polytubes) in vivo in the absence of other phage proteins. The diameter of these structures was the same as the diameter of the tail of phage NBD2 (~12 nm). The length of these structures varied from 0.1 µm to >3.95 µm, which is 23-fold the normal NBD2 tail length. Stability analysis demonstrated that the polytubes could withstand various chemical and physical conditions. These polytubes show the potential to be used as a nanomaterial in various fields of science. ) Array ( [Name] => TypeDocument [Label] => Document Type [Group] => TypDoc [Data] => article ) Array ( [Name] => Format [Label] => File Description [Group] => SrcInfo [Data] => electronic resource ) Array ( [Name] => Language [Label] => Language [Group] => Lang [Data] => English ) Array ( [Name] => ISSN [Label] => ISSN [Group] => ISSN [Data] => 1999-4915<br />11030208 ) Array ( [Name] => NoteTitleSource [Label] => Relation [Group] => SrcInfo [Data] => http://www.mdpi.com/1999-4915/11/3/208; https://doaj.org/toc/1999-4915 ) Array ( [Name] => DOI [Label] => DOI [Group] => ID [Data] => 10.3390/v11030208 ) Array ( [Name] => URL [Label] => Access URL [Group] => URL [Data] => <link linkTarget="URL" linkTerm="https://doaj.org/article/dd9581b8c822443daeb58dae169f4433" linkWindow="_blank">https://doaj.org/article/dd9581b8c822443daeb58dae169f4433</link> ) Array ( [Name] => AN [Label] => Accession Number [Group] => ID [Data] => edsdoj.9581b8c822443daeb58dae169f4433 ) |
RecordInfo |
Array
(
[BibEntity] => Array
(
[Identifiers] => Array
(
[0] => Array
(
[Type] => doi
[Value] => 10.3390/v11030208
)
)
[Languages] => Array
(
[0] => Array
(
[Text] => English
)
)
[PhysicalDescription] => Array
(
[Pagination] => Array
(
[PageCount] => 1
[StartPage] => 208
)
)
[Subjects] => Array
(
[0] => Array
(
[SubjectFull] => bacteriophage vB_EcoS_NBD2
[Type] => general
)
[1] => Array
(
[SubjectFull] => tail tube protein
[Type] => general
)
[2] => Array
(
[SubjectFull] => self-assembly
[Type] => general
)
[3] => Array
(
[SubjectFull] => tubular structure
[Type] => general
)
[4] => Array
(
[SubjectFull] => polytubes
[Type] => general
)
[5] => Array
(
[SubjectFull] => stability
[Type] => general
)
[6] => Array
(
[SubjectFull] => Saccharomyces cerevisiae
[Type] => general
)
[7] => Array
(
[SubjectFull] => Escherichia coli
[Type] => general
)
[8] => Array
(
[SubjectFull] => Microbiology
[Type] => general
)
[9] => Array
(
[SubjectFull] => QR1-502
[Type] => general
)
)
[Titles] => Array
(
[0] => Array
(
[TitleFull] => Self-Assembly of Tail Tube Protein of Bacteriophage vB_EcoS_NBD2 into Extremely Long Polytubes in E. coli and S. cerevisiae
[Type] => main
)
)
)
[BibRelationships] => Array
(
[HasContributorRelationships] => Array
(
[0] => Array
(
[PersonEntity] => Array
(
[Name] => Array
(
[NameFull] => Aliona Špakova
)
)
)
[1] => Array
(
[PersonEntity] => Array
(
[Name] => Array
(
[NameFull] => Eugenijus Šimoliūnas
)
)
)
[2] => Array
(
[PersonEntity] => Array
(
[Name] => Array
(
[NameFull] => Raminta Batiuškaitė
)
)
)
[3] => Array
(
[PersonEntity] => Array
(
[Name] => Array
(
[NameFull] => Simonas Pajeda
)
)
)
[4] => Array
(
[PersonEntity] => Array
(
[Name] => Array
(
[NameFull] => Rolandas Meškys
)
)
)
[5] => Array
(
[PersonEntity] => Array
(
[Name] => Array
(
[NameFull] => Rasa Petraitytė-Burneikienė
)
)
)
)
[IsPartOfRelationships] => Array
(
[0] => Array
(
[BibEntity] => Array
(
[Dates] => Array
(
[0] => Array
(
[D] => 01
[M] => 03
[Type] => published
[Y] => 2019
)
)
[Identifiers] => Array
(
[0] => Array
(
[Type] => issn-print
[Value] => 19994915
)
[1] => Array
(
[Type] => issn-print
[Value] => 11030208
)
)
[Numbering] => Array
(
[0] => Array
(
[Type] => volume
[Value] => 11
)
[1] => Array
(
[Type] => issue
[Value] => 3
)
)
[Titles] => Array
(
[0] => Array
(
[TitleFull] => Viruses
[Type] => main
)
)
)
)
)
)
)
|
IllustrationInfo |