MersV1, PubMed, Checkpoint, bibRecord, 000349

The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping.

Identifieur interne : 000349 ( PubMed/Checkpoint ); précédent : 000348; suivant : 000350

The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping.

Auteurs : Zhemin Zhang [République populaire de Chine] ; Qi Huang [République populaire de Chine] ; Xuan Tao [République populaire de Chine] ; Guobing Song [République populaire de Chine] ; Peng Zheng [République populaire de Chine] ; Hongyan Li ; Hongzhe Sun ; Wei Xia [République populaire de Chine]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2019.

RBID : pubmed:30936204

Descripteurs français

KwdFr :
- Antigènes CD (), Antigènes CD (génétique), Antigènes CD (métabolisme), Cadhérines (), Cadhérines (génétique), Cadhérines (métabolisme), Cristallographie aux rayons X, Domaines protéiques, Facteurs de virulence (), Facteurs de virulence (génétique), Facteurs de virulence (métabolisme), Helicobacter pylori (enzymologie), Helicobacter pylori (génétique), Helicobacter pylori (pathogénicité), Humains, Modèles biologiques, Protéines bactériennes (), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Serine endopeptidases (), Serine endopeptidases (génétique), Serine endopeptidases (métabolisme), Spécificité du substrat.
MESH :
- enzymologie : Helicobacter pylori.
- génétique : Antigènes CD, Cadhérines, Facteurs de virulence, Helicobacter pylori, Protéines bactériennes, Serine endopeptidases.
- métabolisme : Antigènes CD, Cadhérines, Facteurs de virulence, Protéines bactériennes, Serine endopeptidases.
- pathogénicité : Helicobacter pylori.
- Antigènes CD, Cadhérines, Cristallographie aux rayons X, Domaines protéiques, Facteurs de virulence, Humains, Modèles biologiques, Protéines bactériennes, Serine endopeptidases, Spécificité du substrat.

English descriptors

KwdEn :
- Antigens, CD (chemistry), Antigens, CD (genetics), Antigens, CD (metabolism), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Cadherins (chemistry), Cadherins (genetics), Cadherins (metabolism), Crystallography, X-Ray, Helicobacter pylori (enzymology), Helicobacter pylori (genetics), Helicobacter pylori (pathogenicity), Humans, Models, Biological, Protein Domains, Serine Endopeptidases (chemistry), Serine Endopeptidases (genetics), Serine Endopeptidases (metabolism), Substrate Specificity, Virulence Factors (chemistry), Virulence Factors (genetics), Virulence Factors (metabolism).
MESH :
- chemical , chemistry : Antigens, CD, Bacterial Proteins, Cadherins, Serine Endopeptidases, Virulence Factors.
- chemical , genetics : Antigens, CD, Bacterial Proteins, Cadherins, Serine Endopeptidases, Virulence Factors.
- chemical , metabolism : Antigens, CD, Bacterial Proteins, Cadherins, Serine Endopeptidases, Virulence Factors.
- enzymology : Helicobacter pylori.
- genetics : Helicobacter pylori.
- pathogenicity : Helicobacter pylori.
- Crystallography, X-Ray, Humans, Models, Biological, Protein Domains, Substrate Specificity.

Abstract

Knowledge of the molecular mechanisms of specific bacterial virulence factors can significantly contribute to antibacterial drug discovery. Helicobacter pylori is a Gram-negative microaerophilic bacterium that infects almost half of the world's population, leading to gastric disorders and even gastric cancer. H. pylori expresses a series of virulence factors in the host, among which high-temperature requirement A (HpHtrA) is a newly identified serine protease secreted by H. pylori. HpHtrA cleaves the extracellular domain of the epithelial cell surface adhesion protein E-cadherin and disrupts gastric epithelial cell junctions, allowing H. pylori to access the intercellular space. Here we report the first crystal structure of HpHtrA at 3.0 Å resolution. The structure revealed a new type of HtrA protease trimer stabilized by unique N-terminal domain swapping distinct from other known HtrA homologs. We further observed that truncation of the N terminus completely abrogates HpHtrA trimer formation as well as protease activity. In the presence of unfolded substrate, HpHtrA assembled into cage-like 12-mers or 24-mers. Combining crystallographic, biochemical, and mutagenic data, we propose a mechanistic model of how HpHtrA recognizes and cleaves the well-folded E-cadherin substrate. Our study provides a fundamental basis for the development of anti-H. pylori agents by using a previously uncharacterized HtrA protease as a target.

DOI: 10.1074/jbc.RA119.007387
PubMed: 30936204

Affiliations:

République populaire de Chine

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Le document en format XML

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<term>Humans</term>
<term>Models, Biological</term>
<term>Protein Domains</term>
<term>Serine Endopeptidases (chemistry)</term>
<term>Serine Endopeptidases (genetics)</term>
<term>Serine Endopeptidases (metabolism)</term>
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<term>Cadhérines (génétique)</term>
<term>Cadhérines (métabolisme)</term>
<term>Cristallographie aux rayons X</term>
<term>Domaines protéiques</term>
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<term>Modèles biologiques</term>
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<term>Serine Endopeptidases</term>
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<front><div type="abstract" xml:lang="en">Knowledge of the molecular mechanisms of specific bacterial virulence factors can significantly contribute to antibacterial drug discovery. <i>Helicobacter pylori</i>
 is a Gram-negative microaerophilic bacterium that infects almost half of the world's population, leading to gastric disorders and even gastric cancer. <i>H. pylori</i>
 expresses a series of virulence factors in the host, among which high-temperature requirement A (<i>Hp</i>
HtrA) is a newly identified serine protease secreted by <i>H. pylori. Hp</i>
HtrA cleaves the extracellular domain of the epithelial cell surface adhesion protein E-cadherin and disrupts gastric epithelial cell junctions, allowing <i>H. pylori</i>
 to access the intercellular space. Here we report the first crystal structure of <i>Hp</i>
HtrA at 3.0 Å resolution. The structure revealed a new type of HtrA protease trimer stabilized by unique N-terminal domain swapping distinct from other known HtrA homologs. We further observed that truncation of the N terminus completely abrogates <i>Hp</i>
HtrA trimer formation as well as protease activity. In the presence of unfolded substrate, <i>Hp</i>
HtrA assembled into cage-like 12-mers or 24-mers. Combining crystallographic, biochemical, and mutagenic data, we propose a mechanistic model of how <i>Hp</i>
HtrA recognizes and cleaves the well-folded E-cadherin substrate. Our study provides a fundamental basis for the development of anti-<i>H. pylori</i>
 agents by using a previously uncharacterized HtrA protease as a target.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30936204</PMID>
<DateCompleted><Year>2019</Year>
<Month>12</Month>
<Day>09</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>294</Volume>
<Issue>20</Issue>
<PubDate><Year>2019</Year>
<Month>05</Month>
<Day>17</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation>
</Journal>
<ArticleTitle>The unique trimeric assembly of the virulence factor HtrA from <i>Helicobacter pylori</i>
 occurs via N-terminal domain swapping.</ArticleTitle>
<Pagination><MedlinePgn>7990-8000</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA119.007387</ELocationID>
<Abstract><AbstractText>Knowledge of the molecular mechanisms of specific bacterial virulence factors can significantly contribute to antibacterial drug discovery. <i>Helicobacter pylori</i>
 is a Gram-negative microaerophilic bacterium that infects almost half of the world's population, leading to gastric disorders and even gastric cancer. <i>H. pylori</i>
 expresses a series of virulence factors in the host, among which high-temperature requirement A (<i>Hp</i>
HtrA) is a newly identified serine protease secreted by <i>H. pylori. Hp</i>
HtrA cleaves the extracellular domain of the epithelial cell surface adhesion protein E-cadherin and disrupts gastric epithelial cell junctions, allowing <i>H. pylori</i>
 to access the intercellular space. Here we report the first crystal structure of <i>Hp</i>
HtrA at 3.0 Å resolution. The structure revealed a new type of HtrA protease trimer stabilized by unique N-terminal domain swapping distinct from other known HtrA homologs. We further observed that truncation of the N terminus completely abrogates <i>Hp</i>
HtrA trimer formation as well as protease activity. In the presence of unfolded substrate, <i>Hp</i>
HtrA assembled into cage-like 12-mers or 24-mers. Combining crystallographic, biochemical, and mutagenic data, we propose a mechanistic model of how <i>Hp</i>
HtrA recognizes and cleaves the well-folded E-cadherin substrate. Our study provides a fundamental basis for the development of anti-<i>H. pylori</i>
 agents by using a previously uncharacterized HtrA protease as a target.</AbstractText>
<CopyrightInformation>© 2019 Zhang et al.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Zhemin</ForeName>
<Initials>Z</Initials>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Huang</LastName>
<ForeName>Qi</ForeName>
<Initials>Q</Initials>
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</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tao</LastName>
<ForeName>Xuan</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>From the MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Song</LastName>
<ForeName>Guobing</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>the State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zheng</LastName>
<ForeName>Peng</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>the State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.</Affiliation>
</AffiliationInfo>
</Author>
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The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping.

The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping.

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