Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids
Identifieur interne : 000385 ( Ncbi/Merge ); précédent : 000384; suivant : 000386Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids
Auteurs : Paul T. Manna [Royaume-Uni] ; Steven Kelly [Royaume-Uni] ; Mark C. Field [Royaume-Uni]Source :
- Molecular Phylogenetics and Evolution [ 1055-7903 ] ; 2013.
Abstract
► We identify the adaptin gene cohort from currently available kinetoplastid genomes. ► Further, we present analysis of newly sequenced
Url:
DOI: 10.1016/j.ympev.2013.01.002
PubMed: 23337175
PubMed Central: 3650584
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids</title>
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<series><title level="j">Molecular Phylogenetics and Evolution</title>
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<front><div type="abstract" xml:lang="en"><sec><title>Graphical abstract</title>
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<sec><title>Highlights</title>
<p>► We identify the adaptin gene cohort from currently available kinetoplastid genomes. ► Further, we present analysis of newly sequenced <italic>Trypanosoma grayi</italic>
adaptins. ► We describe the evolutionary history of kinetoplastid adaptins. ► Kinetoplastid adaptin cohorts are compared to major surface protein families. ► Adaptin evolution and immune evasion mechanisms are correlated in salivarian trypanosomes.</p>
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</TEI>
<pmc article-type="brief-report"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Mol Phylogenet Evol</journal-id>
<journal-id journal-id-type="iso-abbrev">Mol. Phylogenet. Evol</journal-id>
<journal-title-group><journal-title>Molecular Phylogenetics and Evolution</journal-title>
</journal-title-group>
<issn pub-type="ppub">1055-7903</issn>
<issn pub-type="epub">1095-9513</issn>
<publisher><publisher-name>Academic Press</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">23337175</article-id>
<article-id pub-id-type="pmc">3650584</article-id>
<article-id pub-id-type="publisher-id">S1055-7903(13)00007-9</article-id>
<article-id pub-id-type="doi">10.1016/j.ympev.2013.01.002</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Short Communication</subject>
</subj-group>
</article-categories>
<title-group><article-title>Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Manna</surname>
<given-names>Paul T.</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kelly</surname>
<given-names>Steven</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Field</surname>
<given-names>Mark C.</given-names>
</name>
<email>mcf34@cam.ac.uk</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>a</label>
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK</aff>
<aff id="aff2"><label>b</label>
Oxford Centre for Integrative Systems Biology, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK</aff>
<author-notes><corresp id="cor1"><label>⁎</label>
Corresponding author. <email>mcf34@cam.ac.uk</email>
</corresp>
</author-notes>
<pub-date pub-type="pmc-release"><day>1</day>
<month>4</month>
<year>2013</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>4</month>
<year>2013</year>
</pub-date>
<volume>67</volume>
<issue>1</issue>
<fpage>123</fpage>
<lpage>128</lpage>
<history><date date-type="received"><day>30</day>
<month>10</month>
<year>2012</year>
</date>
<date date-type="rev-recd"><day>20</day>
<month>12</month>
<year>2012</year>
</date>
<date date-type="accepted"><day>7</day>
<month>1</month>
<year>2013</year>
</date>
</history>
<permissions><copyright-statement>© 2013 Elsevier Inc.</copyright-statement>
<copyright-year>2013</copyright-year>
<copyright-holder>Elsevier Inc.</copyright-holder>
<license xlink:href="https://creativecommons.org/licenses/by/3.0/"><license-p>Open Access under <ext-link ext-link-type="uri" xlink:href="https://creativecommons.org/licenses/by/3.0/">CC BY 3.0</ext-link>
license</license-p>
</license>
</permissions>
<abstract abstract-type="graphical"><sec><title>Graphical abstract</title>
<p><fig id="f0015" position="anchor"><graphic xlink:href="fx1"></graphic>
</fig>
</p>
</sec>
<sec><title>Highlights</title>
<p>► We identify the adaptin gene cohort from currently available kinetoplastid genomes. ► Further, we present analysis of newly sequenced <italic>Trypanosoma grayi</italic>
adaptins. ► We describe the evolutionary history of kinetoplastid adaptins. ► Kinetoplastid adaptin cohorts are compared to major surface protein families. ► Adaptin evolution and immune evasion mechanisms are correlated in salivarian trypanosomes.</p>
</sec>
</abstract>
<abstract><p>The kinetoplastids are an important group of protozoa from the Excavata supergroup, and cause numerous diseases with wide environmental, economic and ecological impact. <italic>Trypanosoma brucei</italic>
, the causative agent of human African trypanosomiasis, expresses a dense variant surface glycoprotein (VSG) coat, facilitating immune evasion <italic>via</italic>
rapid switching and antigenic variation. Coupled to VSG switching is efficient clathrin-mediated endocytosis (CME), which removes anti-VSG antibody from the parasite surface. While the precise molecular basis for an extreme CME flux is unknown, genes encoding the AP2 complex, central to CME in most organisms, are absent from <italic>T. brucei</italic>
, suggesting a mechanistic divergence in trypanosome CME. Here we identify the AP complex gene cohorts of all available kinetoplastid genomes and a new <italic>Trypanosoma grayi</italic>
genome. We find multiple secondary losses of AP complexes, but that loss of AP2 is restricted to <italic>T. brucei</italic>
and closest relatives. Further, loss of AP2 correlates precisely with the presence of VSG genes, supporting a model whereby these two adaptations may function synergistically in immune evasion.</p>
</abstract>
<kwd-group><title>Keywords</title>
<kwd>Endocytosis</kwd>
<kwd>Variant surface glycoprotein</kwd>
<kwd>Adaptin</kwd>
<kwd><italic>Trypanosoma grayi</italic>
</kwd>
</kwd-group>
</article-meta>
</front>
<floats-group><fig id="f0005"><label>Fig. 1</label>
<caption><p>Phylogenetic reconstruction of the unique adaptin family γ, α, δ and ε large subunit. The tree shown is the best Bayesian topology with branch support for important nodes indicated. Identified adaptins group reliably by predicted AP complex (see methods) with clades indicated by vertical bars. Note the absence of the AP2 complex α-subunit from all salivarian trypanosomes.</p>
</caption>
<graphic xlink:href="gr1"></graphic>
</fig>
<fig id="f0010"><label>Fig. 2</label>
<caption><p>Reconstruction of AP complex evolutionary history in kinetoplastids. Left side: points of presumed AP complex loss are shown superimposed upon a cladogram based upon the cytosolic HSP90 protein family. Note multiple losses of the AP4 complex and the single loss of AP2 at the base of the extant salivarian trypanosomes, coincident with the emergence of the VSG coat (purple). Dotted lines represent suggested placement of <italic>T. carassii</italic>
and <italic>L. tarentolae</italic>
based on previously reported 18S rRNA gene sequences (<xref rid="b0230 b0240" ref-type="bibr">Stevens et al., 1999; Votypka et al., 2010</xref>
) due to the inability to detect cytosolic HSP90 genes. Right side: Coulson plot of distribution of adaptin and surface antigen (TS: trans-sialidase, AMA: amastin) gene families; genes are represented as columns and taxa as rows. Adaptin subunits are assigned based upon phylogenetic positioning and reciprocal blast analysis. Surface protein families were identified by reciprocal blast (see methods).</p>
</caption>
<graphic xlink:href="gr2"></graphic>
</fig>
</floats-group>
</pmc>
<affiliations><list><country><li>Royaume-Uni</li>
</country>
<region><li>Angleterre</li>
<li>Angleterre de l'Est</li>
<li>Oxfordshire</li>
</region>
<settlement><li>Cambridge</li>
<li>Oxford</li>
</settlement>
<orgName><li>Université d'Oxford</li>
<li>Université de Cambridge</li>
</orgName>
</list>
<tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Manna, Paul T" sort="Manna, Paul T" uniqKey="Manna P" first="Paul T." last="Manna">Paul T. Manna</name>
</region>
<name sortKey="Field, Mark C" sort="Field, Mark C" uniqKey="Field M" first="Mark C." last="Field">Mark C. Field</name>
<name sortKey="Kelly, Steven" sort="Kelly, Steven" uniqKey="Kelly S" first="Steven" last="Kelly">Steven Kelly</name>
</country>
</tree>
</affiliations>
</record>
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