Protein content of the Hylesia metabus egg nest setae (Cramer [1775]) (Lepidoptera: Saturniidae) and its association with the parental investment for the reproductive success and lepidopterism

Cabrera, Gleysin; Lundberg, Ulf; Rodríguez-Ulloa, Arielis; Herrera, Melfrán; Machado, Wendy; Portela, Madelón; Palomares, Sucel; Espinosa, Luis Ariel; Ramos, Yassel; Durán, Rosario; Besada, Vladimir; Vonasek, Eva; González, Luis Javier

doi:10.1016/j.jprot.2016.08.010

Cited by 11 publications

(10 citation statements)

References 52 publications

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“…Because serine proteases have been found to have an important role in mediating the reactions of exposed humans and guinea pigs to the urticating setae of the caterpillars of Euproctis spp. (Bleumink et al 1982) and of the female moths of H. metabus (Lundberg et al 2007;Cabrera et al 2016Cabrera et al , 2017, it would be interesting to assess their role in the T. pityocampa system as well. Serine proteases do occur in the proteome of this species and show some similarity with proteins occurring in Bombyx, Helicoverpa, and Mamestra (Supp.…”

Section: Discussionmentioning

confidence: 99%

“…In both cases, an enzymatic activity (serine protease) seems to occur and appears to be responsible for the typical reaction associated with the contact of human skin with the setae. The presence of several serine proteases has been confirmed in recent proteomic studies by Cabrera et al (2016Cabrera et al ( , 2017 in the setae isolated from the female moths of H. metabus, which are putatively thought to protect the eggs and the young caterpillars from vertebrate predation. This family of proteases represents 65% of the total proteins extracted from the setae of H. metabus.…”

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confidence: 80%

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Proteome Analysis of Urticating Setae From Thaumetopoea pityocampa (Lepidoptera: Notodontidae)

Berardi¹,

Pivato²,

Arrigoni

et al. 2017

Journal of Medical Entomology

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Thaumetopoea pityocampa (Denis & Schiffermüller) (Lepidoptera: Notodontidae) is harmful to conifer trees because of defoliation and to public health because of the release of urticating setae from the caterpillars. Contact with setae by humans and domestic animals induces dermatitis, usually localized to the exposed areas. Recent studies demonstrated the presence of a complex urticating mechanism where proteins present in the setae may play a role as activators of immune responses. Yet, limited information is available at present about the proteins occurring in the setae of T. pityocampa. Using a refined method for protein extraction from the setae, and a combination of liquid chromatography tandem-mass spectrometry (LC-MS/MS), de novo assembly of transcriptomic data, and sequence similarity searches, an extensive data set of 353 proteins was obtained. These were further categorized by molecular function, biological process, and cellular location. All the 353 proteins identified were found to match through BLAST search with at least one Lepidoptera sequence available in databases. We found the previously known allergens Tha p 1 and Tha p 2 described from T. pityocampa, as well as enzymes involved in chitin biosynthesis, one of the principal components of the setae, and serine proteases that were responsible for inflammatory and allergic reactions in other urticating Lepidoptera. This new proteomic database may allow for a better understanding of the complexity of allergenic reactions due to T. pityocampa and to other Lepidoptera sharing similar defense systems.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 80%

Proteome Analysis of Urticating Setae From Thaumetopoea pityocampa (Lepidoptera: Notodontidae)

Berardi¹,

Pivato²,

Arrigoni

et al. 2017

Journal of Medical Entomology

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“…Manual interpretation of the MS/MS spectra were conducted to extract a reliable sequence tag that was confirmed using the b n and y″ n backbone fragment ions. The mass accuracy (0.01–0.02 Da), as well as other aspects used in the de novo sequencing of peptides were also considered to extract this partial sequence [ 46 , 47 ]. The conotoxin of interest was identified in the transcriptome database with the aid of MASCOT [ 25 ], using the sequence query option.…”

Section: Methodsmentioning

confidence: 99%

Antimycobacterial Activity: A New Pharmacological Target for Conotoxins Found in the First Reported Conotoxin from Conasprella ximenes

Figueroa-Montiel

Bernáldez

Jiménez

et al. 2018

Toxins

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Mycobacterium tuberculosis is the etiological agent of tuberculosis, an airborne infectious disease that is a leading cause of human morbidity and mortality worldwide. We report here the first conotoxin that is able to inhibit the growth of M. tuberculosis at a concentration similar to that of two other drugs that are currently used in clinics. Furthermore, it is also the first conopeptide that has been isolated from the venom of Conasprella ximenes. The venom gland transcriptome of C. ximenes was sequenced to construct a database with 24,284 non-redundant transcripts. The conopeptide was purified from the venom using reverse phase high performance liquid chromatography (RP-HPLC) and was analyzed using electrospray ionization-mass spectrometry (ESI-MS/MS). No automatic identification above the identity threshold with 1% of the false discovery rate was obtained; however, a 10-amino-acid sequence tag, manually extracted from the MS/MS spectra, allowed for the identification of a conotoxin in the transcriptome database. Electron transfer higher energy collision dissociation (EThcD) fragmentation of the native conotoxin confirmed the N-terminal sequence (1–14), while LC-MS/MS analysis of the tryptic digest of the reduced and S-alkylated conotoxin confirmed the C-terminal region (15–36). The expected and experimental molecular masses corresponded, within sub-ppm mass error. The 37-mer peptide (MW 4109.69 Da), containing eight cysteine residues, was named I1_xm11a, according to the current nomenclature for this type of molecule.

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“…N-glycans are able to stabilize the 3D structure and/or optimize the enzyme-substrate binding by ionic interaction. In a subsequent research by Cabrera et al (2017) [67], the authors could identify that the protein content of the setae is dominated by enzymes. More specifically, using SDS-PAGE analysis, they could identify that 65% of the venom content is represented by five proteases with homology to S1A serine proteases [67].…”

Section: Edema and Erythemamentioning

confidence: 96%

“…In a subsequent research by Cabrera et al (2017) [67], the authors could identify that the protein content of the setae is dominated by enzymes. More specifically, using SDS-PAGE analysis, they could identify that 65% of the venom content is represented by five proteases with homology to S1A serine proteases [67]. The function of these S1A serine proteases still needs more investigation, although for one of the proteases, HM-PT60, the function was already described as mentioned above [30].…”

Section: Edema and Erythemamentioning

confidence: 96%

Caterpillar Venom: A Health Hazard of the 21st Century

2020

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Caterpillar envenomation is a global health threat in the 21st century. Every direct or indirect contact with the urticating hairs of a caterpillar results in clinical manifestations ranging from local dermatitis symptoms to potentially life-threatening systemic effects. This is mainly due to the action of bioactive components in the venom that interfere with targets in the human body. The problem is that doctors are limited to relieve symptoms, since an effective treatment is still lacking. Only for Lonomia species an effective antivenom does exist. The health and economical damage are an underestimated problem and will be even more of a concern in the future. For some caterpillar species, the venom composition has been the subject of investigation, while for many others it remains unknown. Moreover, the targets involved in the pathophysiology are poorly understood. This review aims to give an overview of the knowledge we have today on the venom composition of different caterpillar species along with their pharmacological targets. Epidemiology, mode of action, clinical time course and treatments are also addressed. Finally, we briefly discuss the future perspectives that may open the doors for future research in the world of caterpillar toxins to find an adequate treatment.

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Protein content of the Hylesia metabus egg nest setae (Cramer [1775]) (Lepidoptera: Saturniidae) and its association with the parental investment for the reproductive success and lepidopterism

Cited by 11 publications

References 52 publications

Proteome Analysis of Urticating Setae From Thaumetopoea pityocampa (Lepidoptera: Notodontidae)

Proteome Analysis of Urticating Setae From Thaumetopoea pityocampa (Lepidoptera: Notodontidae)

Antimycobacterial Activity: A New Pharmacological Target for Conotoxins Found in the First Reported Conotoxin from Conasprella ximenes

Caterpillar Venom: A Health Hazard of the 21st Century

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