Thermoregulatory behaviour and thermal tolerance of three species of Conidae in the Eastern Pacific and Gulf of California coasts of Baja California, Mexico

Lugo-Fabres, Pavel H.; Dı́az, Fernando; Re, Ana Denisse; Olivares, Félix; González, Ricardo Bonilla; Dueñas, Salvador; Licea-Navarro, Alexei F.

doi:10.1080/13235818.2016.1172545

Cited by 3 publications

(1 citation statement)

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“…Specimens of Conasprella ximenes , a mollusk-hunting cone snail [ 41 ], were collected from the sandy sublittoral area of Bahía de Los Angeles, Ensenada, Baja California, Mexico. The organisms were identified by means of mitochondrial 16S sequence.…”

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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Section: Methodsmentioning

confidence: 99%