From crystal structure to in silico epitope discovery in the Burkholderia pseudomallei flagellar hook‐associated protein FlgK
Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to th...
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| Published in | The FEBS journal Vol. 282; no. 7; pp. 1319 - 1333 |
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| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
01.04.2015
Blackwell Publishing Ltd |
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| Abstract | Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook‐associated protein (FlgKBₚ), and provides the first insights into the 3D structure of FlgK proteins as targets for structure‐based antigen engineering. The FlgKBₚcrystal structure (presented here at 1.8‐Å resolution) reveals a multidomain fold, comprising two small β‐domains protruding from a large elongated α‐helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook‐associated proteins are likely to show a conserved, elongated α‐helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgKBₚ, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgKBₚhas cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgKBₚcrystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgKBₚas a candidate for the design and production of epitope‐containing subunits/domains as potential vaccine components. |
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| AbstractList | Melioidosis, caused by the Gram‐negative bacterium
Burkholderia pseudomallei
, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the
B. pseudomallei
flagellar hook‐associated protein (Flg
K
B
p
), and provides the first insights into the 3D structure of FlgK proteins as targets for structure‐based antigen engineering. The Flg
K
B
p
crystal structure (presented here at 1.8‐Å resolution) reveals a multidomain fold, comprising two small β‐domains protruding from a large elongated α‐helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook‐associated proteins are likely to show a conserved, elongated α‐helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against Flg
K
B
p
, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that Flg
K
B
p
has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the Flg
K
B
p
crystal structure, coupled with
in vitro
mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to Flg
K
B
p
as a candidate for the design and production of epitope‐containing subunits/domains as potential vaccine components. Melioidosis, caused by the Gram-negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook-associated protein (FlgK(Bp)), and provides the first insights into the 3D structure of FlgK proteins as targets for structure-based antigen engineering. The FlgK(Bp) crystal structure (presented here at 1.8-Å resolution) reveals a multidomain fold, comprising two small β-domains protruding from a large elongated α-helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook-associated proteins are likely to show a conserved, elongated α-helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgK(Bp), in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgK(Bp) has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgK(Bp) crystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgK(Bp) as a candidate for the design and production of epitope-containing subunits/domains as potential vaccine components.Melioidosis, caused by the Gram-negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook-associated protein (FlgK(Bp)), and provides the first insights into the 3D structure of FlgK proteins as targets for structure-based antigen engineering. The FlgK(Bp) crystal structure (presented here at 1.8-Å resolution) reveals a multidomain fold, comprising two small β-domains protruding from a large elongated α-helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook-associated proteins are likely to show a conserved, elongated α-helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgK(Bp), in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgK(Bp) has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgK(Bp) crystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgK(Bp) as a candidate for the design and production of epitope-containing subunits/domains as potential vaccine components. Melioidosis, caused by the Gram-negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook-associated protein (FlgK(Bp)), and provides the first insights into the 3D structure of FlgK proteins as targets for structure-based antigen engineering. The FlgK(Bp) crystal structure (presented here at 1.8-Å resolution) reveals a multidomain fold, comprising two small β-domains protruding from a large elongated α-helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook-associated proteins are likely to show a conserved, elongated α-helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgK(Bp), in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgK(Bp) has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgK(Bp) crystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgK(Bp) as a candidate for the design and production of epitope-containing subunits/domains as potential vaccine components. Melioidosis, caused by the Gram-negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook-associated protein (FlgKBp), and provides the first insights into the 3D structure of FlgK proteins as targets for structure-based antigen engineering. The FlgKBp crystal structure (presented here at 1.8-Aa resolution) reveals a multidomain fold, comprising two small beta -domains protruding from a large elongated alpha -helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook-associated proteins are likely to show a conserved, elongated alpha -helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgKBp, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgKBp has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgKBp crystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgKBp as a candidate for the design and production of epitope-containing subunits/domains as potential vaccine components. We present the crystal structure of the B. pseudomallei flagellar hook-associated protein (FlgKBp) and show that it is a seroreactive antigen and cytotoxic towards murine macrophages. Using in silico and in vitro methods, we mapped potential epitopes to discrete FlgKBp domains that indicate FlgKBp as a potential target for structure-based antigen design and melioidosis vaccine discovery. Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook‐associated protein (FlgKBₚ), and provides the first insights into the 3D structure of FlgK proteins as targets for structure‐based antigen engineering. The FlgKBₚcrystal structure (presented here at 1.8‐Å resolution) reveals a multidomain fold, comprising two small β‐domains protruding from a large elongated α‐helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook‐associated proteins are likely to show a conserved, elongated α‐helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgKBₚ, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgKBₚhas cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgKBₚcrystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgKBₚas a candidate for the design and production of epitope‐containing subunits/domains as potential vaccine components. Melioidosis, caused by the Gram-negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook-associated protein (FlgKBp), and provides the first insights into the 3D structure of FlgK proteins as targets for structure-based antigen engineering. The FlgKBp crystal structure (presented here at 1.8-Å resolution) reveals a multidomain fold, comprising two small [beta]-domains protruding from a large elongated [alpha]-helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook-associated proteins are likely to show a conserved, elongated [alpha]-helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgKBp, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgKBp has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgKBp crystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgKBp as a candidate for the design and production of epitope-containing subunits/domains as potential vaccine components. Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook‐associated protein (FlgKBₚ), and provides the first insights into the 3D structure of FlgK proteins as targets for structure‐based antigen engineering. The FlgKBₚcrystal structure (presented here at 1.8‐Å resolution) reveals a multidomain fold, comprising two small β‐domains protruding from a large elongated α‐helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook‐associated proteins are likely to show a conserved, elongated α‐helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgKBₚ, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgKBₚhas cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgKBₚcrystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgKBₚas a candidate for the design and production of epitope‐containing subunits/domains as potential vaccine components. Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern Australia that is poorly controlled by antibiotics. Research efforts to identify antigenic components for a melioidosis vaccine have led to the identification of several proteins, including subunits forming the flagella that mediate bacterial motility, host colonization, and virulence. This study focuses on the B. pseudomallei flagellar hook‐associated protein (FlgKBp), and provides the first insights into the 3D structure of FlgK proteins as targets for structure‐based antigen engineering. The FlgKBp crystal structure (presented here at 1.8‐Å resolution) reveals a multidomain fold, comprising two small β‐domains protruding from a large elongated α‐helical bundle core. The evident structural similarity to flagellin, the flagellar filament subunit protein, suggests that, depending on the bacterial species, flagellar hook‐associated proteins are likely to show a conserved, elongated α‐helical bundle scaffold coupled to a variable number of smaller domains. Furthermore, we present immune serum recognition data confirming, in agreement with previous findings, that recovered melioidosis patients produce elevated levels of antibodies against FlgKBp, in comparison with seronegative and seropositive healthy subjects. Moreover, we show that FlgKBp has cytotoxic effects on cultured murine macrophages, suggesting an important role in bacterial pathogenesis. Finally, computational epitope prediction methods applied to the FlgKBp crystal structure, coupled with in vitro mapping, allowed us to predict three antigenic regions that locate to discrete protein domains. Taken together, our results point to FlgKBp as a candidate for the design and production of epitope‐containing subunits/domains as potential vaccine components. We present the crystal structure of the B. pseudomallei flagellar hook‐associated protein (FlgKBp) and show that it is a seroreactive antigen and cytotoxic towards murine macrophages. Using in silico and in vitro methods, we mapped potential epitopes to discrete FlgKBp domains that indicate FlgKBp as a potential target for structure‐based antigen design and melioidosis vaccine discovery. |
| Author | Gourlay, Louise J Thomas, Rachael J Colombo, Giorgio Nithichanon, Arnone Ferrer‐Navarro, Mario Titball, Richard Lertmemongkolchai, Ganjana Bolognesi, Martino Conchillo‐Solé, Oscar Daura, Xavier Vila, Jordi Peri, Claudio |
| Author_xml | – sequence: 1 fullname: Gourlay, Louise J – sequence: 2 fullname: Thomas, Rachael J – sequence: 3 fullname: Peri, Claudio – sequence: 4 fullname: Conchillo‐Solé, Oscar – sequence: 5 fullname: Ferrer‐Navarro, Mario – sequence: 6 fullname: Nithichanon, Arnone – sequence: 7 fullname: Vila, Jordi – sequence: 8 fullname: Daura, Xavier – sequence: 9 fullname: Lertmemongkolchai, Ganjana – sequence: 10 fullname: Titball, Richard – sequence: 11 fullname: Colombo, Giorgio – sequence: 12 fullname: Bolognesi, Martino |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25645451$$D View this record in MEDLINE/PubMed |
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| Keywords | flagellar hook-associated protein antigen epitope discovery structural vaccinology Burkholderia pseudomallei |
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| Snippet | Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern... Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei , is a potentially fatal infection that is endemic in Southeast Asia and Northern... Melioidosis, caused by the Gram-negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern... Melioidosis, caused by the Gram‐negative bacterium Burkholderia pseudomallei, is a potentially fatal infection that is endemic in Southeast Asia and Northern... |
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| SubjectTerms | Amino Acid Sequence Animals antibiotics antibodies Antibodies, Bacterial - blood antigen Antigens, Bacterial - chemistry antiserum Australia bacterial motility Bacterial Proteins - chemistry Bacterial Proteins - immunology Bacterial Proteins - physiology Burkholderia pseudomallei Burkholderia pseudomallei - immunology Burkholderia pseudomallei Cell Line Computer Simulation Crystal structure Crystallography, X-Ray cytotoxicity engineering epitope discovery epitopes Epitopes - chemistry flagellar hook‐associated protein flagellin flagellum Gram-negative bacteria Humans Immunoglobulins macrophages Macrophages - immunology Macrophages - microbiology melioidosis Melioidosis - blood Melioidosis - immunology Melioidosis - microbiology Mice Models, Molecular Molecular Sequence Data pathogenesis patients prediction protein subunits Proteins seroprevalence South East Asia structural vaccinology Vaccines virulence |
| Title | From crystal structure to in silico epitope discovery in the Burkholderia pseudomallei flagellar hook‐associated protein FlgK |
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