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[[Image:Pertussis_toxin_complex.png|thumb|left|300px|Cartoon representation of the molecular structure of pertussis toxin.]] | [[Image:Pertussis_toxin_complex.png|thumb|left|300px|Cartoon representation of the molecular structure of pertussis toxin.]] | ||
'''Pertussis Toxin (PTX)''' is a toxin produced and secreted by the bacteria ''Bordetella pertussis'', also known as the [http://en.wikipedia.org/wiki/Whooping_cough whooping cough] agent. | '''Pertussis Toxin (PTX)''' is a toxin produced and secreted by the bacteria [http://fr.wikipedia.org/wiki/Bordetella_pertussis ''Bordetella pertussis''], also known as the [http://en.wikipedia.org/wiki/Whooping_cough whooping cough] agent. | ||
It is a complex soluble bacterial [[:wiktionary:holotoxin|Holotoxin]], composed of 5 subuntits (named S1 to S5 according to their decreasing molecular weights), arranged in an A-B structure. The A part contains the enzymatically active <scene name='56/568016/Ptx_s1/1'>S1</scene> subunit, which catalyzes ADP-ribosylation of α subunit of [http://en.wikipedia.org/wiki/G_protein trimeric G proteins], thereby disturbing major metabolic functions of the target cells, leading to a variety of biological activities. | It is a complex soluble bacterial [[:wiktionary:holotoxin|Holotoxin]], composed of 5 subuntits (named S1 to S5 according to their decreasing molecular weights), arranged in an A-B structure. The A part contains the enzymatically active <scene name='56/568016/Ptx_s1/1'>S1</scene> subunit, which catalyzes ADP-ribosylation of α subunit of [http://en.wikipedia.org/wiki/G_protein trimeric G proteins], thereby disturbing major metabolic functions of the target cells, leading to a variety of biological activities. | ||
The <scene name='56/568016/Ptx_b/1'>B oligomer</scene> is composed by <scene name='56/568016/Ptx_s2/2'>1S2</scene>:<scene name='56/568016/Ptx_s3/1'>1S3</scene>:<scene name='56/568016/Ptx_s4/1'>2S4</scene>:<scene name='56/568016/Ptx_s5/1'>1S5</scene> and is responsible for binding of the toxin to target cell receptors and for intracellular traficking. | The <scene name='56/568016/Ptx_b/1'>B oligomer</scene> is composed by <scene name='56/568016/Ptx_s2/2'>1S2</scene>:<scene name='56/568016/Ptx_s3/1'>1S3</scene>:<scene name='56/568016/Ptx_s4/1'>2S4</scene>:<scene name='56/568016/Ptx_s5/1'>1S5</scene> and is responsible for binding of the toxin to target cell receptors and for intracellular traficking. | ||
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PMID:7901213 | PMID:7901213 | ||
</ref> | </ref> | ||
have been identified: His35 is involved in the ionization of the nucleophilic thiol of the cysteine residue in the G protein via its ε-N | have been identified: His35 is involved in the ionization of the nucleophilic thiol of the cysteine residue in the G protein via its ε-N <ref name="Transit">PMID:9204866</ref>and the carboxylate group of the <scene name='56/568016/Ptx_glu129/1'>Glu129</scene> side chain is in contact with the 2'-ribo-hydroxyl of the NAD<sup>+</sup> | ||
<ref name="Antoine95"> | <ref name="Antoine95"> | ||
PMID:8527486 | PMID:8527486 | ||
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==Structural informations allow to produce efficient vaccine== | ==Structural informations allow to produce efficient vaccine== | ||
Crystal structure provided insight into the pathogenic mechanisms of PTX. Informations about the tertiary structure of the active site is a good basis for elimination of the catalytic activity in recombinant molecules for vaccine use. | |||
For example, one highly detoxified PTX analog contains two alterations in the S1 subunit (Arg9 to Lys; Glu129 to Gly), each of which is able to totally abolish the enzymativ activity of the toxin. This molecule already belongs to the new-generation of pertussis vaccines <ref name="Karzon90">PMID:2190139</ref>. | For example, one highly detoxified PTX analog contains two alterations in the S1 subunit (Arg9 to Lys; Glu129 to Gly), each of which is able to totally abolish the enzymativ activity of the toxin. This molecule already belongs to the new-generation of pertussis vaccines <ref name="Karzon90">PMID:2190139</ref>. | ||
==See Also== | ==See Also== | ||
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==Proteopedia Page Contributors and Editors== | ==Proteopedia Page Contributors and Editors== | ||
[[User:Paul Giroud|Paul Giroud]] | [[User:Lea Clusan|Lea Clusan]] and [[User:Paul Giroud|Paul Giroud]] | ||
