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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Myriapod haemocyanin: the first three-dimensional reconstruction of Scolopendra subspinipes and preliminary structural analysis of S. viridicornis

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Author(s):
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Riciluca, K. C. T. [1, 2] ; Borges, A. C. [1] ; Mello, J. F. R. [1] ; de Oliveira, U. C. [2] ; Serdan, D. C. [1] ; Florez-Ariza, A. [1] ; Chaparro, E. [2, 3] ; Nishiyama-Jr, M. Y. ; Cassago, A. [1] ; Junqueira-de-Azevedo, I. L. M. [4] ; van Heel, M. [1] ; Silva Jr, I, P. ; Portugal, V, R.
Total Authors: 13
Affiliation:
[1] V, CNPEM, Lab Nacl Nanotecnol LNNano, BR-13083970 Campinas, SP - Brazil
[2] I, Ctr Toxinas Imunoresposta & Sinalizacao Celular C, Inst Butantan, Lab Toxinol Aplicada LETA, Sao Paulo - Brazil
[3] I, Univ Sao Paulo, Interunidades Biotecnol, Sao Paulo - Brazil
[4] Nishiyama-Jr, Jr., M. Y., I, Ctr Toxinas Imunoresposta & Sinalizacao Celular C, Inst Butantan, Lab Toxinol Aplicada LETA, Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: OPEN BIOLOGY; v. 10, n. 4 APR 1 2020.
Web of Science Citations: 0
Abstract

Haemocyanins (Hcs) are copper-containing, respiratory proteins that occur in the haemolymph of many arthropod species. Here, we report the presence of Hcs in the chilopode Myriapoda, demonstrating that these proteins are more widespread among the Arthropoda than previously thought. The analysis of transcriptome of S. subspinipes subpinipes reveals the presence of two distinct subunits of Hc, where the signal peptide is present, and six of prophenoloxidase (PPO), where the signal peptide is absent, in the 75 kDa range. Size exclusion chromatography profiles indicate different quaternary organization for Hc of both species, which was corroborated by TEM analysis: S. viridicornis Hc is a 6 x 6-mer and S. subspinipes Hc is a 3 x 6-mer, which resembles the half-structure of the 6 x 6-mer but also includes the presence of phenoloxidases, since the 1 x 6-mer quaternary organization is commonly associated with hexamers of PPO. Studies with Chelicerata showed that PPO activity are exclusively associated with the Hcs. This study indicates that Scolopendra may have different proteins playing oxygen transport (Hc) and PO function, both following the hexameric oligomerization observed in Hcs. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 17/15340-2 - EMU: acquisition of a transmission electron microscope for single particle cryo electron microscopy - establishing a cryo electron microscopy open facility at CNPEM
Grantee:Rodrigo Villares Portugal
Support Opportunities: Multi-user Equipment Program