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<StructureSection load='1MA2' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>
<StructureSection load='' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>
== Introduction ==
== Introduction ==
Tachyplesin I (TP-I) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth  of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].
'''Tachyplesin I, II and III''' are [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth  of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].
The antimicrobial activity of the polypeptide is contributed by electrostatic interaction between the negatively charged membrane of bacteria and fungi to positively charged part of <scene name='67/671725/Cationic_peptide_tpi/3'> TP-I </scene> <ref name=Laederach>PMID:12369825</ref> (see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Charge_Cationic}} amino acids).
The antimicrobial activity of the polypeptide is contributed by electrostatic interaction between the negatively charged membrane of bacteria and fungi to positively charged part of <scene name='67/671725/Cationic_peptide_tpi/3'> TP-I </scene> <ref name=Laederach>PMID:12369825</ref> (see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Charge_Cationic}} amino acids).
Specifically, TP-I shows high affinity for negatively charged [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects.  
Specifically, TP-I shows high affinity for negatively charged [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects.  
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[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water  surrounding</scene>  to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>.
[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water  surrounding</scene>  to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>.


== Derivatives or Analogue ==
== Derivatives or Analogue ==
Among all the existing interactions, the cysteine bridges were considered as the principal contributors of the hairpin loop structure. To test this, three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues were systematically replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below:
Among all the existing interactions, the cysteine bridges were considered as the principal contributors of the hairpin loop structure. To test this, three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues were systematically replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below:


[[Image:Seq TPI.jpg|750px]]
[[Image:Seq TPI.jpg|500px]]


Of these 3 linear derivatives of TP-I, NMR structural investigations had shown that TPA4 was unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapt hairpin loop structure and also retain their antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of LPS and its biological activities.
Of these 3 linear derivatives of TP-I, NMR structural investigations had shown that TPA4 was unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapt hairpin loop structure and also retain their antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of LPS and its biological activities.
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<b><u> Plants and Agriculture </u></b>
<b><u> Plants and Agriculture </u></b>


Evidences suggest that TP-I has ability to permeabilize the cell membranes of pathogens.<ref name=Laederach>PMID:12369825</ref>. Also, LPS and DNA being the potential biological targets of the peptide, its antimicrobial activity might be exploited. Eyeing the potential of TP-I, it has been insetred successfully in genome of ''Ornithogalum dubium'' and ''Ornithogalum thyrsoides''. These ornamentals plants were originally sensitive to soft rot erwinias (SREs) and insertion of TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref>.
Evidences suggest that TP-I has ability to permeabilize the cell membranes of pathogens.<ref name=Laederach>PMID:12369825</ref>. Also, LPS and DNA being the potential biological targets of the peptide, its antimicrobial activity might be exploited. Eyeing the potential of TP-I, it has been insetred successfully in genome of ''Ornithogalum dubium'' and ''Ornithogalum thyrsoides''. These ornamentals plants were originally sensitive to soft rot erwinias (SREs) and insertion of TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref><ref name=Lipsky and Joshi>PMID:27639550</ref>.


<b><u> Clinical Importance </u></b>
<b><u> Clinical Importance </u></b>
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==3D structure of tachyplesin==
==3D structure of tachyplesin==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


[[1ma2]], [[1ma5]], [[1wo0]], [[1wo1]], [[2mdb]], [[2rtv]] – TacI peptide residues 24-40  – Japanese horseshoe crab - NMR<br />
*Tachyplesin I 
[[1ma4]], [[1ma6]] – TacI peptide residues 24-40 (mutant) - NMR<br />
[[2lm8]] – TacI peptide residues 1-13 (mutant) - NMR<br />


**[[1ma2]], [[1ma5]], [[1wo0]], [[1wo1]], [[2mdb]], [[2rtv]], [[6pin]] – TtTacI peptide residues 24-40  – Tachypleus tridentatus -  - NMR<br />
**[[1ma4]], [[1ma6]] – TtTacI peptide residues 24-40 (mutant) - NMR<br />
**[[2lm8]] – TacI peptide residues 1-13 (mutant) - NMR<br />


*Tachyplesin II 
**[[6pio]] – TtTacII peptide residues 24-40  - NMR<br />
**[[6pi2]] – TacII peptide residues 24-40  - Limulus polyphemus - NMR<br />
*Tachyplesin III 
**[[6pip]], [[6pi3]] – TacIII + peptide residues 24-40  - Tachypleus gigas - NMR<br />
}}


== Quiz ==
== Quiz ==
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</Quiz>
</Quiz>
</StructureSection>


== References ==
== References ==
<references/>
<references/>
</StructureSection>
[[Category:Topic Page]]
[[Category:Pages with quizzes]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Janak Raj Joshi, Shulamit Idzikowski, Michal Harel, Alexander Berchansky, Joel L. Sussman, Angel Herraez, Jaime Prilusky
Retrieved from "https://proteopedia.openfox.io/w/Tachyplesin"