Urumin

Urumin is a naturally occurring 27-amino acid virucidal host defense peptide against the human influenza A virus.[1] It was discovered and isolated from the skin of Hydrophylax bahuvistara, a species of frog found in South India, by a team of Emory University researchers.[1] The team that discovered urumin tested the peptide against 8 different H1N1 and 4 different H3N2 viruses, as well as various other influenza viruses.[1] The peptide specifically targets the evolutionarily conserved H1 hemagglutinin stalk region of H1-containing influenza A viruses.[1] Additionally, urumin was active against drug-resistant influenza A viruses, that were resistant against oseltamivir, zanamivir and peramivir .[1] While its mechanism of action is not fully understood, urumin seems to inhibit viral growth by physically destroying influenza A virions, and is able to protect naive mice from doses of influenza A infection as high as 2 times the LD50.[1] Because of its specific targeting of the hemagglutinin stalk region of the influenza A virus, the mechanism of action of urumin is similar to that of antibodies induced in the body by universal influenza vaccines.[1] Urumin was also tested for toxicity against erythrocytes and showed a TD50 of 2,450 μM and TI of 664.7, indicating a favorable toxicity profile against erythrocytes.[1] As such, urumin may represent the basis for a potential first-line antiviral treatment against influenza A, particularly in the context of influenza outbreaks,[1] although the discoverers of the peptide have stated that urumin is far from becoming an anti-flu drug.[2] Urumin was named after Urumi, a sword used in Kalaripayattu, the martial art of Kerala, where it was discovered.[3]

Urumin
Names
Other names
IPLRGAFINGRWDSQCHRFSNGAIACA; H-Ile-Pro-Leu-Arg-Gly-Ala-Phe-Ile-Asn-Gly-Arg-Trp-Asp-Ser-Gln-Cys-His-Arg-Phe-Ser-Asn-Gly-Ala-Ile-Ala-Cys-Ala-OH
Identifiers
3D model (JSmol)
  • InChI=1S/C129H198N42O35S2/c1-13-63(6)100(133)125(204)171-43-27-37-92(171)122(201)163-80(44-62(4)5)112(191)154-76(34-24-40-141-127(134)135)106(185)145-54-96(177)149-66(9)103(182)157-82(46-71-30-20-17-21-31-71)117(196)170-102(65(8)15-3)124(203)164-86(50-95(132)176)108(187)147-56-98(179)153-77(35-25-41-142-128(136)137)109(188)159-83(47-72-52-144-75-33-23-22-32-74(72)75)114(193)162-87(51-99(180)181)116(195)166-88(57-172)118(197)156-79(38-39-93(130)174)111(190)168-91(60-208)121(200)160-84(48-73-53-140-61-148-73)115(194)155-78(36-26-42-143-129(138)139)110(189)158-81(45-70-28-18-16-19-29-70)113(192)165-89(58-173)119(198)161-85(49-94(131)175)107(186)146-55-97(178)150-67(10)105(184)169-101(64(7)14-2)123(202)151-68(11)104(183)167-90(59-207)120(199)152-69(12)126(205)206/h16-23,28-33,52-53,61-69,76-92,100-102,144,172-173,207-208H,13-15,24-27,34-51,54-60,133H2,1-12H3,(H2,130,174)(H2,131,175)(H2,132,176)(H,140,148)(H,145,185)(H,146,186)(H,147,187)(H,149,177)(H,150,178)(H,151,202)(H,152,199)(H,153,179)(H,154,191)(H,155,194)(H,156,197)(H,157,182)(H,158,189)(H,159,188)(H,160,200)(H,161,198)(H,162,193)(H,163,201)(H,164,203)(H,165,192)(H,166,195)(H,167,183)(H,168,190)(H,169,184)(H,170,196)(H,180,181)(H,205,206)(H4,134,135,141)(H4,136,137,142)(H4,138,139,143)/t63-,64-,65-,66-,67-,68-,69-,76-,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,100-,101-,102-/m0/s1
    Key: QLPKBNCTTOVOBP-QZGABZBFSA-N
  • N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)NCC(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(=O)N)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(C)C(=O)O
Properties
C129H198N42O35S2
Molar mass 2961.38 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

References

  1. Holthausen DJ, Lee SH, Kumar VT, Bouvier NM, Krammer F, Ellebedy AH, Wrammert J, Lowen AC, George S, Pillai MR, Jacob J (2017). "An Amphibian Host Defense Peptide Is Virucidal for Human H1 Hemagglutinin-Bearing Influenza Viruses". Immunity. 46 (4): 587–595. doi:10.1016/j.immuni.2017.03.018. PMID 28423338.
  2. SciNews (2017). "Frog Skin Peptide 'Urumin' Kills H1 Influenza Viruses".
  3. Healy, Melissa (18 April 2017). "Why the next flu medicine could come from frog mucus". Los Angeles Times. Retrieved 7 January 2021.


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