Tags

Type your tag names separated by a space and hit enter

Characterization of the excretory/secretory products of Dermatobia hominis larvae, the human bot fly.
Vet Parasitol. 2010 Mar 25; 168(3-4):304-11.VP

Abstract

Proteolytic activity in excretory/secretory products (ESP) of first- (L1), second- (L2) and third-instar (L3) larvae of Dermatobia hominis was analyzed through gelatin-gel and colorimetric enzyme assays with the chromogenic substrates azocasein and BApNA. The functional characterization of proteases was based on inhibition assays including synthetic inhibitors. ESP were obtained from new-hatched larvae reared in the laboratory and from second- and third-instar larvae removed from naturally infested cattle. Gelatin-gel analysis evidenced few bands of proteolysis, predominantly of high apparent molecular masses, in ESP of L1, whereas in the gel of L2 and L3 ESP there was a wide range of proteolytic activity most of them not resolved in a single species. Azocasein assays revealed a progressive increase of protease activity from first- to third-instar larvae. Protease inhibitor assays revealed a predominance of metalloproteases in L1 ESP that could be related to a skin penetration process and to a diversion of host immune response. The predominance of serine proteases in L2 and L3 and the great tryptic activity presented by L3 ESP were attributed to an increasing trophic activity by the growing larvae, since the viability of adult flies strictly depends on larval abilities to assimilate nutrients from the host. Taking together, these results suggest that Dematobia larvae secrete/excrete different proteases that may be related to diverse functions during host penetration and infestation, which reinforces the relevance of the study of such proteolytic enzymes.

Links

Publisher Full Text

Authors+Show Affiliations

Brant MP
Curso de Pós-graduação - Faculdade de Medicina Veterinária e Zootecnia - Unesp, Botucatu, SP, Brazil.
Guimarães S
No affiliation info available
Souza-Neto JA
No affiliation info available
Ribolla PE
No affiliation info available
Oliveira-Sequeira TC
No affiliation info available

MeSH

AnimalsCattleCattle DiseasesDipteraEctoparasitic InfestationsEnzyme ActivationFemaleHumansLarvaPeptide HydrolasesProtease Inhibitors

Pub Type(s)

Journal Article

Language

eng

PubMed ID

20042295

Citation

Brant, M P R., et al. "Characterization of the Excretory/secretory Products of Dermatobia Hominis Larvae, the Human Bot Fly." Veterinary Parasitology, vol. 168, no. 3-4, 2010, pp. 304-11.
Brant MP, Guimarães S, Souza-Neto JA, et al. Characterization of the excretory/secretory products of Dermatobia hominis larvae, the human bot fly. Vet Parasitol. 2010;168(3-4):304-11.
Brant, M. P., Guimarães, S., Souza-Neto, J. A., Ribolla, P. E., & Oliveira-Sequeira, T. C. (2010). Characterization of the excretory/secretory products of Dermatobia hominis larvae, the human bot fly. Veterinary Parasitology, 168(3-4), 304-11. https://doi.org/10.1016/j.vetpar.2009.11.018
Brant MP, et al. Characterization of the Excretory/secretory Products of Dermatobia Hominis Larvae, the Human Bot Fly. Vet Parasitol. 2010 Mar 25;168(3-4):304-11. PubMed PMID: 20042295.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of the excretory/secretory products of Dermatobia hominis larvae, the human bot fly. AU - Brant,M P R, AU - Guimarães,S, AU - Souza-Neto,J A, AU - Ribolla,P E M, AU - Oliveira-Sequeira,T C G, Y1 - 2009/12/01/ PY - 2009/06/04/received PY - 2009/11/05/revised PY - 2009/11/25/accepted PY - 2010/1/1/entrez PY - 2010/1/1/pubmed PY - 2010/6/16/medline SP - 304 EP - 11 JF - Veterinary parasitology JO - Vet Parasitol VL - 168 IS - 3-4 N2 - Proteolytic activity in excretory/secretory products (ESP) of first- (L1), second- (L2) and third-instar (L3) larvae of Dermatobia hominis was analyzed through gelatin-gel and colorimetric enzyme assays with the chromogenic substrates azocasein and BApNA. The functional characterization of proteases was based on inhibition assays including synthetic inhibitors. ESP were obtained from new-hatched larvae reared in the laboratory and from second- and third-instar larvae removed from naturally infested cattle. Gelatin-gel analysis evidenced few bands of proteolysis, predominantly of high apparent molecular masses, in ESP of L1, whereas in the gel of L2 and L3 ESP there was a wide range of proteolytic activity most of them not resolved in a single species. Azocasein assays revealed a progressive increase of protease activity from first- to third-instar larvae. Protease inhibitor assays revealed a predominance of metalloproteases in L1 ESP that could be related to a skin penetration process and to a diversion of host immune response. The predominance of serine proteases in L2 and L3 and the great tryptic activity presented by L3 ESP were attributed to an increasing trophic activity by the growing larvae, since the viability of adult flies strictly depends on larval abilities to assimilate nutrients from the host. Taking together, these results suggest that Dematobia larvae secrete/excrete different proteases that may be related to diverse functions during host penetration and infestation, which reinforces the relevance of the study of such proteolytic enzymes. SN - 1873-2550 UR - https://www.unboundmedicine.com/medline/citation/20042295/Characterization_of_the_excretory/secretory_products_of_Dermatobia_hominis_larvae_the_human_bot_fly_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0304-4017(09)00696-7 DB - PRIME DP - Unbound Medicine ER -