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ABSTRACT The pathogens transmitted by ticks to human beings are a motive of public health concern around the world, such is the case of Lyme disease in the northern hemisphere, Encephalitis virus in Europe, the recurrent fevers and the Rocky Mountains spotted fever, better known in Colombia as "Tobia Fever". People of all economic and social conditions are prone to develop a zoonotic agent transmitted by these vectors, which could be infected by several pathogens through co-infection mechanisms. The epidemiology and prevalence of these diseases are affected by ecological, climatic and anthropogenic factors. All these factors, affect in a different manner the enzootic cycle between pathogens, ticks and wild hosts. Current molecular diagnostic tools have allowed to progress in pathogen identification, previously unknown or undetermined. The government intervention capacity of each country, and the multidisciplinary professional cooperation, especially from physicians and veterinarians, is fundamental in order to strategically implement control and prevention plans that can deal with this problematic. The present article aims to make a thorough review of the factors which are favoring the transmission of zoonotic agents by ticks, contextualizing the most important aspects that determine their prevalence, and the most relevant control and prevention measures.

Classification problems of functional data arise naturally in many applications. Several approaches have been considered for solving the problem of finding groups based on functional data. In this paper, we are interested in detecting groups when the functional data are spatially correlated. Our methodology allows to find spatially homogeneous groups of sites when the observations at each sampling location consist of samples of random functions. In univariable and multivariable geostatistics, various methods of incorporating spatial information into the clustering analysis have been considered. Here, we extend these methods to the functional context to fulfil the task of clustering spatially correlated curves. In our approach, we initially use basis functions to smooth the observed data, and then, we weight the dissimilarity matrix among curves by either the trace‐variogram or the multivariable variogram calculated with the coefficients of the basis functions. This paper contains a simulation study as well as the analysis of a real data set corresponding to average daily temperatures measured at 35 Canadian weather stations.

Understanding protein amyloidogenesis is an important topic in protein science, fueled by the role of amyloid aggregates, especially oligomers, in the etiology of a number of devastating human degenerative diseases. However, the mechanisms that determine the formation of amyloid oligomers remain elusive due to the high complexity of the amyloidogenesis process. For instance, gold nanoparticles promote or inhibit amyloid fibrillation. We have functionalized gold nanorods with a metal-chelating group to selectively immobilize soluble RepA-WH1, a model synthetic bacterial prionoid, using a hexa-histidine tag (H6). H6-RepA-WH1 undergoes stable amyloid oligomerization in the presence of catalytic concentrations of anisotropic nanoparticles. Then, in a physically separated event, such oligomers promote the growth of amyloid fibers of untagged RepA-WH1. SERS spectral changes of H6-RepA-WH1 on spherical citrate-AuNP substrates provide evidence for structural modifications in the protein, which are compatible with a gradual increase in ?-sheet structure, as expected in amyloid oligomerization. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ; Research at RG laboratory was supported by MINECO grants CSD2009-00088 and BIO2012-30852. Research at AGM and LMLM laboratories was supported by MINECO (MAT2014-59678-R and MAT2013-46101-R) and Madrid Regional Government (S2013/MIT-2807) grants. A.G.-M. and G.G.-R., respectively, acknowledge receipt of Ramón y Cajal and FPI Fellowships from the Spanish MINECO.

21 p.-3 fig.-1 tab.-9 fig. supl. ; Understanding protein amyloidogenesis is an important topic in protein science, fueled by the role of amyloid aggregates, especially oligomers, in the etiology of a number of devastating human degenerative diseases. However, the mechanisms that determine the formation of amyloid oligomers remain elusive due to the high complexity of the amyloidogenesis process. For instance, gold nanoparticles promote or inhibit amyloid fibrillation. We have functionalized gold nanorods with a metal-chelating group to selectively immobilize soluble RepA-WH1, a model synthetic bacterial prionoid, using a hexa-histidine tag (H6). H6-RepA-WH1 undergoes stable amyloid oligomerization in the presence of catalytic concentrations of anisotropic nanoparticles. Then, in a physically separated event, such oligomers promote the growth of amyloid fibers of untagged RepA-WH1. SERS spectral changes of H6-RepA-WH1 on spherical citrate-AuNP substrates provide evidence for structural modifications in the protein, which are compatible with a gradual increase in β-sheet structure, as expected in amyloid oligomerization. ; Research at the R.G.laboratory was supported by MINECO grants CSD2009-00088, BIO2012-30852 and BIO2015-68730-R. Research at the A.G-M. and L.M.L-M. laboratories was supported by MINECO (MAT2014-59678-R and MAT2013-46101-R), Madrid Regional Government (S2013/MIT-2807) and the "I Convocatoria de Ayudas Fundación BBVA a Investigadores,Innovadores y Creadores Culturales"(14_CBB_147) grants.A.G-M. and G.G-R. acknowledge,respectively,receipt of Ramón y Cajal and FPI Fellowships from the Spanish MINECO. ; Peer reviewed

Most available structures of amyloids correspond to peptide fragments that self-assemble in extended cross b sheets. However, structures in which a whole protein domain acts as building block of an amyloid fiber are scarce, in spite of their relevance to understand amyloidogenesis. Here, we use electron microscopy (EM) and atomic force microscopy (AFM) to analyze the structure of amyloid filaments assembled by RepA-WH1, a winged-helix domain from a DNA replication initiator in bacterial plasmids. RepA-WH1 functions as a cytotoxic bacterial prionoid that recapitulates features of mammalian amyloid proteinopathies. RepA are dimers that monomerize at the origin to initiate replication, and we find that RepA-WH1 reproduces this transition to form amyloids. RepA-WH1 assembles double helical filaments by lateral association of a singlestranded precursor built by monomers. Double filaments then associate in mature fibers. The intracellular and cytotoxic RepA-WH1 aggregates might reproduce the hierarchical assembly of human amyloidogenic proteins. ; This work was supported by grants of the Spanish Government SAF2011- 22988 and the Autonomous Region of Madrid S2010/BMD-2316 to O.L.; BIO2012-30852 and CSD2009-00088 to R.G.; BFU2011-25090 to J.M.-B.; and FIS2011-24638 and ERC Starting grant ref 206117 to F.M.-H. ; Peer reviewed