scholarly journals Geographic Distribution of Ehrlichia Canis Genotypes in Brazil

2020 ◽  
Author(s):  
Isis Taques ◽  
Amanda Campos ◽  
Mayara Kavazaki ◽  
Sayanne Almeida ◽  
Daniel Aguiar
Keyword(s):  
Geographic Distribution ◽  
Tandem Repeat ◽  
Costa Rican ◽  
Ehrlichia Canis ◽  
Tropical Region ◽  
The South ◽  
Serum Samples ◽  
Temperate Region ◽  
Repeat Proteins ◽  
Tandem Repeat Proteins

Tandem repeat proteins of 36 kDa (TRP36) are major immunoreactive proteins of Ehrlichia canis, which have been used in the serological diagnosis of different genotypes of the microorganism. The aim of this study was to evaluate the distribution of the American (USTRP36), Brazilian (BrTRP36) and Costa Rican (CRTRP36) genotypes of E. canis in Brazil, using ELISA assays. Serum samples of 815 dogs from 49 cities from all over Brazil were analyzed. Our results showed that 33.9% of the samples were reactive to the USTRP36 genotype and 32.6% to the BrTRP36 genotype. The two genotypes appeared to occur equally throughout Brazil, although the frequency of seropositivity was lower in the south than in the country’s other regions. Co-positivity for the American and Brazilian genotypes was also observed in 16% of samples. A few dogs (n=5; 0.6%) reactive to E. canis-TRP36 genotype (CRTRP36) were also detected in the northeast and southern regions. We conclude that the American and Brazilian genotypes of E. canis are distributed evenly in Brazil, especially in the tropical region, while the temperate region in the south presented the lowest prevalence values. This study offers the first report of dogs seropositive for the Costa Rican genotype in Brazil.

scholarly journals Geographic Distribution of Ehrlichia canis TRP Genotypes in Brazil

2020 ◽  
Vol 7 (4) ◽  
pp. 165
Author(s):  
Isis Indaiara Gonçalves Granjeiro Taques ◽  
Amanda Noeli Silva Campos ◽  
Mayara Lima Kavasaki ◽  
Sayanne Luns Hatum de Almeida ◽  
Daniel Moura de Aguiar
Keyword(s):  
Synthetic Peptides ◽  
Costa Rican ◽  
Ehrlichia Canis ◽  
Dense Core ◽  
Tropical Region ◽  
The South ◽  
Serum Samples ◽  
Temperate Region ◽  
Repeat Proteins ◽  
Tandem Repeat Proteins

Tandem repeat proteins (TRPs) are major immunoreactive proteins of Ehrlichia canis, which have been used in the serological diagnosis of different genotypes of the microorganism. TRP19 is preserved among different E. canis isolates expressed on both reticulate and dense-core cells and observed in the extracellular matrix or associated with the morula membrane. TRP36 is differentially expressed only on the surface of the dense-core form of the bacterium and exhibits more divergence among isolates. The aim of this study was to evaluate the distribution of the American (USTRP36), Brazilian (BrTRP36) and Costa Rican (CRTRP36) genotypes of E. canis in Brazil, using ELISA assays. Serum samples of 814 dogs from 49 municipalities from all over Brazil were analyzed. Our results showed that 34% of the samples were reactive to the USTRP36 genotype and 32.6% to the BrTRP36 genotype. The two genotypes appeared to occur equally throughout Brazil, although the frequency of seropositivity was lower in the south than in the country’s other regions. Dogs that reacted to at least one of the synthetic peptides (TRP19 and TRP36) were 456 (56%). A few dogs (n = 5; 0.61%) reactive to the E. canis TRP36 genotype (CRTRP36) were also detected in the northeast and southern regions. We concluded that the American and Brazilian genotypes of E. canis are distributed evenly in Brazil, especially in the tropical region, while the temperate region in the south presented the lowest prevalence rates. This study offers the first report of dogs seropositive for the Costa Rican genotype in Brazil.

scholarly journals Identification of new silk-like protein from B. magister and development of functional materials based on it

2021 ◽  
Vol 2086 (1) ◽  
pp. 012123
Author(s):  
A A Vronskaia ◽  
A D Mikushina ◽  
I E Eliseev
Keyword(s):  
Thin Films ◽  
Drug Delivery ◽  
Tandem Repeat ◽  
Composite Structure ◽  
Textile Industry ◽  
Functional Materials ◽  
Repeat Proteins ◽  
Tandem Repeat Proteins ◽  
New Protein

Abstract Tandem repeat proteins have composite structure and unique properties, which allow them to be used in multiple fields, such as soft photonics, drug delivery and textile industry. The recent discovery of squid ring teeth (SRT) proteins have expanded the existing repertoire of repetitive polypeptides. We chose previously unexplored squid B. magister for our research, isolated and analyzed a new protein forming its ring teeth and hooks, and amplified the corresponding gene. Finally, we used this new isolated SRT protein to fabricate transparent thin films and microspheres.

scholarly journals Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs

2019 ◽  
Vol 116 (29) ◽  
pp. 14456-14464 ◽  
Author(s):  
Spencer A. Hughes ◽  
Fengbin Wang ◽  
Shengyuan Wang ◽  
Mark A. B. Kreutzberger ◽  
Tomasz Osinski ◽  
...  
Keyword(s):  
Tandem Repeat ◽  
Self Assembly ◽  
Sequence Similarity ◽  
Structural Data ◽  
Consensus Sequences ◽  
Repeat Proteins ◽  
Helical Hairpin ◽  
Tandem Repeat Proteins ◽  
Helical Protein ◽  
Helical Geometry

Tandem repeat proteins exhibit native designability and represent potentially useful scaffolds for the construction of synthetic biomimetic assemblies. We have designed 2 synthetic peptides, HEAT_R1 and LRV_M3Δ1, based on the consensus sequences of single repeats of thermophilic HEAT (PBS_HEAT) and Leucine-Rich Variant (LRV) structural motifs, respectively. Self-assembly of the peptides afforded high-aspect ratio helical nanotubes. Cryo-electron microscopy with direct electron detection was employed to analyze the structures of the solvated filaments. The 3D reconstructions from the cryo-EM maps led to atomic models for the HEAT_R1 and LRV_M3Δ1 filaments at resolutions of 6.0 and 4.4 Å, respectively. Surprisingly, despite sequence similarity at the lateral packing interface, HEAT_R1 and LRV_M3Δ1 filaments adopt the opposite helical hand and differ significantly in helical geometry, while retaining a local conformation similar to previously characterized repeat proteins of the same class. The differences in the 2 filaments could be rationalized on the basis of differences in cohesive interactions at the lateral and axial interfaces. These structural data reinforce previous observations regarding the structural plasticity of helical protein assemblies and the need for high-resolution structural analysis. Despite these observations, the native designability of tandem repeat proteins offers the opportunity to engineer novel helical nanotubes. Moreover, the resultant nanotubes have independently addressable and chemically distinguishable interior and exterior surfaces that would facilitate applications in selective recognition, transport, and release.

Mechanical Properties of Tandem-Repeat Proteins Are Governed by Network Defects

2018 ◽  
Vol 4 (3) ◽  
pp. 884-891 ◽  
Author(s):  
Abdon Pena-Francesch ◽  
Huihun Jung ◽  
Mo Segad ◽  
Ralph H. Colby ◽  
Benjamin D. Allen ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Tandem Repeat ◽  
Repeat Proteins ◽  
Tandem Repeat Proteins

scholarly journals Dissecting and reprogramming the folding and assembly of tandem-repeat proteins

2015 ◽  
Vol 43 (5) ◽  
pp. 881-888 ◽  
Author(s):  
Pamela J.E. Rowling ◽  
Elin M. Sivertsson ◽  
Albert Perez-Riba ◽  
Ewan R.G. Main ◽  
Laura S. Itzhaki
Keyword(s):  
Protein Design ◽  
Tandem Repeat ◽  
Rational Design ◽  
Topological Complexity ◽  
Energy Barriers ◽  
Step Size ◽  
Repeat Proteins ◽  
Tandem Repeat Proteins ◽  
Level Of Understanding ◽  
Modular Structures

Studying protein folding and protein design in globular proteins presents significant challenges because of the two related features, topological complexity and co-operativity. In contrast, tandem-repeat proteins have regular and modular structures composed of linearly arrayed motifs. This means that the biophysics of even giant repeat proteins is highly amenable to dissection and to rational design. Here we discuss what has been learnt about the folding mechanisms of tandem-repeat proteins. The defining features that have emerged are: (i) accessibility of multiple distinct routes between denatured and native states, both at equilibrium and under kinetic conditions; (ii) different routes are favoured for folding compared with unfolding; (iii) unfolding energy barriers are broad, reflecting stepwise unravelling of an array repeat by repeat; (iv) highly co-operative unfolding at equilibrium and the potential for exceptionally high thermodynamic stabilities by introducing consensus residues; (v) under force, helical-repeat structures are very weak with non-co-operative unfolding leading to elasticity and buffering effects. This level of understanding should enable us to create repeat proteins with made-to-measure folding mechanisms, in which one can dial into the sequence the order of repeat folding, number of pathways taken, step size (co-operativity) and fine-structure of the kinetic energy barriers.

scholarly journals DeepSymmetry: using 3D convolutional networks for identification of tandem repeats and internal symmetries in protein structures

2019 ◽  
Vol 35 (24) ◽  
pp. 5113-5120 ◽  
Author(s):  
Guillaume Pagès ◽  
Sergei Grudinin
Keyword(s):  
Tandem Repeat ◽  
Tandem Repeats ◽  
Protein Structures ◽  
Molecular Structures ◽  
Supplementary Information ◽  
Convolutional Networks ◽  
Repeat Proteins ◽  
Density Maps ◽  
Tandem Repeat Proteins ◽  
Internal Symmetries

Abstract Motivation Thanks to the recent advances in structural biology, nowadays 3D structures of various proteins are solved on a routine basis. A large portion of these structures contain structural repetitions or internal symmetries. To understand the evolution mechanisms of these proteins and how structural repetitions affect the protein function, we need to be able to detect such proteins very robustly. As deep learning is particularly suited to deal with spatially organized data, we applied it to the detection of proteins with structural repetitions. Results We present DeepSymmetry, a versatile method based on 3D convolutional networks that detects structural repetitions in proteins and their density maps. Our method is designed to identify tandem repeat proteins, proteins with internal symmetries, symmetries in the raw density maps, their symmetry order and also the corresponding symmetry axes. Detection of symmetry axes is based on learning 6D Veronese mappings of 3D vectors, and the median angular error of axis determination is less than one degree. We demonstrate the capabilities of our method on benchmarks with tandem-repeated proteins and also with symmetrical assemblies. For example, we have discovered about 7800 putative tandem repeat proteins in the PDB. Availability and implementation The method is available at https://team.inria.fr/nano-d/software/deepsymmetry. It consists of a C++ executable that transforms molecular structures into volumetric density maps, and a Python code based on the TensorFlow framework for applying the DeepSymmetry model to these maps. Supplementary information Supplementary data are available at Bioinformatics online.

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