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The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii
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| Zeitschriftentitel: | mBio |
|---|---|
| Personen und Körperschaften: | , , |
| In: | mBio, 11, 2020, 1 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
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| Schlagwörter: |
| author_facet |
Lopez, Juvenal Ly, Pek Man Feldman, Mario F. Lopez, Juvenal Ly, Pek Man Feldman, Mario F. |
|---|---|
| author |
Lopez, Juvenal Ly, Pek Man Feldman, Mario F. |
| spellingShingle |
Lopez, Juvenal Ly, Pek Man Feldman, Mario F. mBio The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii Virology Microbiology |
| author_sort |
lopez, juvenal |
| spelling |
Lopez, Juvenal Ly, Pek Man Feldman, Mario F. 2161-2129 2150-7511 American Society for Microbiology Virology Microbiology http://dx.doi.org/10.1128/mbio.02761-19 <jats:p> Despite the clinical relevance of <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> , little is known about its fundamental biology. Here, we show that a single amino acid mutation in VgrG, a critical T6SS structural protein, abrogates T6SS function. Given that this mutation was found in a clinical isolate, we propose that the T6SS of <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> is probably not involved in virulence; this idea is supported by multiple genomic analyses showing that the majority of clinical <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> strains lack proteins essential to the T6SS. We also show that, unlike in other species, the C terminus of VgrG is a unique architectural requirement for functional T6SS assembly in <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> , suggesting that over evolutionary time, bacteria have developed changes to their T6SS architecture, leading to specialized systems. </jats:p> The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in <i>Acinetobacter baumannii</i> mBio |
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| title |
The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_unstemmed |
The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_full |
The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_fullStr |
The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_full_unstemmed |
The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_short |
The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_sort |
the tip of the vgrg spike is essential to functional type vi secretion system assembly in
<i>acinetobacter baumannii</i> |
| topic |
Virology Microbiology |
| url |
http://dx.doi.org/10.1128/mbio.02761-19 |
| publishDate |
2020 |
| physical |
|
| description |
<jats:p>
Despite the clinical relevance of
<jats:named-content content-type="genus-species">A. baumannii</jats:named-content>
, little is known about its fundamental biology. Here, we show that a single amino acid mutation in VgrG, a critical T6SS structural protein, abrogates T6SS function. Given that this mutation was found in a clinical isolate, we propose that the T6SS of
<jats:named-content content-type="genus-species">A. baumannii</jats:named-content>
is probably not involved in virulence; this idea is supported by multiple genomic analyses showing that the majority of clinical
<jats:named-content content-type="genus-species">A. baumannii</jats:named-content>
strains lack proteins essential to the T6SS. We also show that, unlike in other species, the C terminus of VgrG is a unique architectural requirement for functional T6SS assembly in
<jats:named-content content-type="genus-species">A. baumannii</jats:named-content>
, suggesting that over evolutionary time, bacteria have developed changes to their T6SS architecture, leading to specialized systems.
</jats:p> |
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| author | Lopez, Juvenal, Ly, Pek Man, Feldman, Mario F. |
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| description | <jats:p> Despite the clinical relevance of <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> , little is known about its fundamental biology. Here, we show that a single amino acid mutation in VgrG, a critical T6SS structural protein, abrogates T6SS function. Given that this mutation was found in a clinical isolate, we propose that the T6SS of <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> is probably not involved in virulence; this idea is supported by multiple genomic analyses showing that the majority of clinical <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> strains lack proteins essential to the T6SS. We also show that, unlike in other species, the C terminus of VgrG is a unique architectural requirement for functional T6SS assembly in <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> , suggesting that over evolutionary time, bacteria have developed changes to their T6SS architecture, leading to specialized systems. </jats:p> |
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| spelling | Lopez, Juvenal Ly, Pek Man Feldman, Mario F. 2161-2129 2150-7511 American Society for Microbiology Virology Microbiology http://dx.doi.org/10.1128/mbio.02761-19 <jats:p> Despite the clinical relevance of <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> , little is known about its fundamental biology. Here, we show that a single amino acid mutation in VgrG, a critical T6SS structural protein, abrogates T6SS function. Given that this mutation was found in a clinical isolate, we propose that the T6SS of <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> is probably not involved in virulence; this idea is supported by multiple genomic analyses showing that the majority of clinical <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> strains lack proteins essential to the T6SS. We also show that, unlike in other species, the C terminus of VgrG is a unique architectural requirement for functional T6SS assembly in <jats:named-content content-type="genus-species">A. baumannii</jats:named-content> , suggesting that over evolutionary time, bacteria have developed changes to their T6SS architecture, leading to specialized systems. </jats:p> The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in <i>Acinetobacter baumannii</i> mBio |
| spellingShingle | Lopez, Juvenal, Ly, Pek Man, Feldman, Mario F., mBio, The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii, Virology, Microbiology |
| title | The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_full | The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_fullStr | The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_full_unstemmed | The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_short | The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| title_sort | the tip of the vgrg spike is essential to functional type vi secretion system assembly in <i>acinetobacter baumannii</i> |
| title_unstemmed | The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii |
| topic | Virology, Microbiology |
| url | http://dx.doi.org/10.1128/mbio.02761-19 |