scholarly journals Pan-Genome Analysis of Vibrio cholerae and Vibrio metschnikovii Strains Isolated From Migratory Birds at Dali Nouer Lake in Chifeng, China

2021 ◽  
Vol 8 ◽  
Author(s):  
Lin Zheng ◽  
Ling-Wei Zhu ◽  
Jie Jing ◽  
Jia-yao Guan ◽  
Ge-Jin Lu ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Matrix Protein ◽  
Migratory Birds ◽  
Migratory Bird ◽  
Extracellular Matrix Protein ◽  
Pan Genome ◽  
Vibrio Metschnikovii ◽  
Inner Mongolia Autonomous Region ◽  
First Time ◽  
Core Genes

Migratory birds are recently recognized as Vibrio disease vectors, but may be widespread transporters of Vibrio strains. We isolated Vibrio cholerae (V. cholerae) and Vibrio metschnikovii (V. metschnikovii) strains from migratory bird epidemic samples from 2017 to 2018 and isolated V. metschnikovii from migratory bird feces in 2019 from bird samples taken from the Inner Mongolia autonomous region of China. To investigate the evolution of these two Vibrio species, we sequenced the genomes of 40 V. cholerae strains and 34 V. metschnikovii strains isolated from the bird samples and compared these genomes with reference strain genomes. The pan-genome of all V. cholerae and V. metschnikovii genomes was large, with strains exhibiting considerable individual differences. A total of 2,130 and 1,352 core genes were identified in the V. cholerae and V. metschnikovii genomes, respectively, while dispensable genes accounted for 16,180 and 9,178 of all genes for the two strains, respectively. All V. cholerae strains isolated from the migratory birds that encoded T6SS and hlyA were non-O1/O139 serotypes without the ability to produce CTX. These strains also lacked the ability to produce the TCP fimbriae nor the extracellular matrix protein RbmA and could not metabolize trimetlylamine oxide (TMAO). Thus, these characteristics render them unlikely to be pandemic-inducing strains. However, a V. metschnikovii isolate encoding the complete T6SS system was isolated for the first time. These data provide new molecular insights into the diversity of V. cholerae and V. metschnikovii isolates recovered from migratory birds.

scholarly journals The 1.9 Å crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion

2019 ◽  
Vol 294 (40) ◽  
pp. 14499-14511 ◽  
Author(s):  
Katherine Kaus ◽  
Alison Biester ◽  
Ethan Chupp ◽  
Jianyi Lu ◽  
Charlie Visudharomn ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Extracellular Matrix ◽  
Vibrio Cholerae ◽  
Matrix Protein ◽  
Bacterial Biofilm ◽  
Extracellular Matrix Protein

1280: Increased Susceptibility to Genitovaginal Prolapse Associated with a Polymorphism in the Promoter of the Extracellular Matrix Protein LAMC1

2007 ◽  
Vol 177 (4S) ◽  
pp. 421-422
Author(s):  
Ganka Nikolova ◽  
Christian O. Twiss ◽  
Hane Lee ◽  
Nelson Stanley ◽  
Janet Sinsheimer ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Increased Susceptibility

scholarly journals Homogenous overexpression of the extracellular matrix protein Netrin-1 in a hollow fiber bioreactor

2021 ◽  
Author(s):  
Aniel Moya-Torres ◽  
Monika Gupta ◽  
Fabian Heide ◽  
Natalie Krahn ◽  
Scott Legare ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hollow Fiber ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Continuous Production ◽  
Extracellular Matrix Protein ◽  
Close Monitoring ◽  
High Quality ◽  
Biolayer Interferometry ◽  
Hollow Fiber Bioreactor

Abstract The production of recombinant proteins for functional and biophysical studies, especially in the field of structural determination, still represents a challenge as high quality and quantities are needed to adequately perform experiments. This is in part solved by optimizing protein constructs and expression conditions to maximize the yields in regular flask expression systems. Still, work flow and effort can be substantial with no guarantee to obtain improvements. This study presents a combination of workflows that can be used to dramatically increase protein production and improve processing results, specifically for the extracellular matrix protein Netrin-1. This proteoglycan is an axon guidance cue which interacts with various receptors to initiate downstream signaling cascades affecting cell differentiation, proliferation, metabolism, and survival. We were able to produce large glycoprotein quantities in mammalian cells, which were engineered for protein overexpression and secretion into the media using the controlled environment provided by a hollow fiber bioreactor. Close monitoring of the internal bioreactor conditions allowed for stable production over an extended period of time. In addition to this, Netrin-1 concentrations were monitored in expression media through biolayer interferometry which allowed us to increase Netrin-1 media concentrations tenfold over our current flask systems while preserving excellent protein quality and in solution behavior. Our particular combination of genetic engineering, cell culture system, protein purification, and biophysical characterization permitted us to establish an efficient and continuous production of high-quality protein suitable for structural biology studies that can be translated to various biological systems. Key points • Hollow fiber bioreactor produces substantial yields of homogenous Netrin-1 • Biolayer interferometry allows target protein quantitation in expression media • High production yields in the bioreactor do not impair Netrin-1 proteoglycan quality Graphical abstract

scholarly journals Atlas of ticks (Acari: Argasidae, Ixodidae) in Germany

2021 ◽  
Author(s):  
Franz Rubel ◽  
Katharina Brugger ◽  
Lidia Chitimia-Dobler ◽  
Hans Dautel ◽  
Elisabeth Meyer-Kayser ◽  
...  
Keyword(s):  
Tick Species ◽  
Migratory Birds ◽  
Dermacentor Reticulatus ◽  
Ixodid Ticks ◽  
Federal States ◽  
Ixodes Frontalis ◽  
Argas Reflexus ◽  
The One ◽  
Argasid Tick ◽  
First Time

AbstractAn updated and increased compilation of georeferenced tick locations in Germany is presented here. This data collection extends the dataset published some years ago by another 1448 new tick locations, 900 locations of which were digitized from literature and 548 locations are published here for the first time. This means that a total of 3492 georeferenced tick locations is now available for Germany. The tick fauna of Germany includes two species of Argasidae in the genera Argas and Carios and 19 species of Ixodidae in the genera Dermacentor, Haemaphysalis, and Ixodes, altogether 21 tick species. In addition, three species of Ixodidae in the genera Hyalomma (each spring imported by migratory birds) and Rhipicephalus (occasionally imported by dogs returning from abroad with their owners) are included in the tick atlas. Of these, the georeferenced locations of 23 tick species are depicted in maps. The occurrence of the one remaining tick species, the recently described Ixodes inopinatus, is given at the level of the federal states. The most common and widespread tick species is Ixodes ricinus, with records in all 16 federal states. With the exception of Hamburg, Dermacentor reticulatus was also found in all federal states. The occurrence of the ixodid ticks Ixodes canisuga, Ixodes frontalis, Ixodes hexagonus and I. inopinatus were documented in at least 11 federal states each. The two mentioned argasid tick species were also documented in numerous federal states, the pigeon tick Argas reflexus in 11 and the bat tick Carios vespertilionis in seven federal states. The atlas of ticks in Germany and the underlying digital dataset in the supplement can be used to improve global tick maps or to study the effects of climate change and habitat alteration on the distribution of tick species.

scholarly journals Specific heparan sulfate modifications stabilize the synaptic organizer MADD-4/Punctin at C. elegans neuromuscular junctions

Genetics ◽  
2021 ◽  
Author(s):  
Mélissa Cizeron ◽  
Laure Granger ◽  
Hannes E BÜlow ◽  
Jean-Louis Bessereau
Keyword(s):  
Heparan Sulfate ◽  
Matrix Protein ◽  
Neuromuscular Junctions ◽  
Core Protein ◽  
Extracellular Matrix Protein ◽  
Inhibitory Synapses ◽  
Single Chain ◽  
C Elegans ◽  
Sugar Chains

Abstract Heparan sulfate proteoglycans contribute to the structural organization of various neurochemical synapses. Depending on the system, their role involves either the core protein or the glycosaminoglycan chains. These linear sugar chains are extensively modified by heparan sulfate modification enzymes, resulting in highly diverse molecules. Specific modifications of glycosaminoglycan chains may thus contribute to a sugar code involved in synapse specificity. Caenorhabditis elegans is particularly useful to address this question because of the low level of genomic redundancy of these enzymes, as opposed to mammals. Here, we systematically mutated the genes encoding heparan sulfate modification enzymes in C. elegans and analyzed their impact on excitatory and inhibitory neuromuscular junctions. Using single chain antibodies that recognize different heparan sulfate modification patterns, we show in vivo that these two heparan sulfate epitopes are carried by the SDN-1 core protein, the unique C. elegans syndecan orthologue, at neuromuscular junctions. Intriguingly, these antibodies differentially bind to excitatory and inhibitory synapses, implying unique heparan sulfate modification patterns at different neuromuscular junctions. Moreover, while most enzymes are individually dispensable for proper organization of neuromuscular junctions, we show that 3-O-sulfation of SDN-1 is required to maintain wild-type levels of the extracellular matrix protein MADD-4/Punctin, a central synaptic organizer that defines the identity of excitatory and inhibitory synaptic domains at the plasma membrane of muscle cells.

scholarly journals Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21

1997 ◽  
Vol 16 (5) ◽  
pp. 289-292 ◽  
Author(s):  
Maureen R. Johnson ◽  
Douglas J. Wilkin ◽  
Hans L. Vos ◽  
Rosa Isela Ortiz De Luna ◽  
Anindya M. Dehejia ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Extracellular Matrix Protein 1 ◽  
Chromosome 1Q21
Sign in / Sign up

Export Citation Format

Share Document