scholarly journals Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega

2011 ◽  
Vol 7 (1) ◽  
pp. 539 ◽  
Author(s):  
Fabian Sievers ◽  
Andreas Wilm ◽  
David Dineen ◽  
Toby J Gibson ◽  
Kevin Karplus ◽  
...  
Author(s):  
P. Sumitha ◽  
K. Sukumar ◽  
S. Srivignesh

Eggshell apex abnormality (EAA) associated with Mycoplasma synoviae is occurring regularly in many commercial layer chicken farms of Tamil Nadu. Choanal cleft swabs were collected from EAA affected poultry farms, subjected for isolation and molecular detection of M. synoviae. Among 16 farms investigated M. synoviae could be isolated in six farms. All the farms were positive for M. synoviae in PCR. Among six isolates three isolates (VCandRI-NKL-SV3, VCandRI-NKL- PV6, VCandRI-NKL-KV2) from severe clinical outbreak were sequenced for vlhA gene and compared with the available sequences from the Gene Bank (NCBI) using multiple sequence alignments software - Clustal Omega and Bio edit programs. Analysis showed that the VCandRI,NKL-SV3 and VCandRI-NKL-KV2 were more similar (94.3%) to each other. Point mutation percentage of isolates VCandRI-NKL-PV6, VCandRI-NKL-SV3 and VCandRI-NKL-KV2 isolates in comparison with reference strain KC506806 were 12, 5.1 and 1.8% respectively. The phylogenetic analysis indicated that the VCandRI-NKL-SV3 and VCandRI-NKL-PV6 were closely evolved with VCandRI-NKL-KV2. VCandRI-NKL-KV2 was closely related to sequence of Mycoplasma synoviae from Brazil.


2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Elena N. Judd ◽  
Alison R. Gilchrist ◽  
Nicholas R. Meyerson ◽  
Sara L. Sawyer

Abstract Background The Type I interferon response is an important first-line defense against viruses. In turn, viruses antagonize (i.e., degrade, mis-localize, etc.) many proteins in interferon pathways. Thus, hosts and viruses are locked in an evolutionary arms race for dominance of the Type I interferon pathway. As a result, many genes in interferon pathways have experienced positive natural selection in favor of new allelic forms that can better recognize viruses or escape viral antagonists. Here, we performed a holistic analysis of selective pressures acting on genes in the Type I interferon family. We initially hypothesized that the genes responsible for inducing the production of interferon would be antagonized more heavily by viruses than genes that are turned on as a result of interferon. Our logic was that viruses would have greater effect if they worked upstream of the production of interferon molecules because, once interferon is produced, hundreds of interferon-stimulated proteins would activate and the virus would need to counteract them one-by-one. Results We curated multiple sequence alignments of primate orthologs for 131 genes active in interferon production and signaling (herein, “induction” genes), 100 interferon-stimulated genes, and 100 randomly chosen genes. We analyzed each multiple sequence alignment for the signatures of recurrent positive selection. Counter to our hypothesis, we found the interferon-stimulated genes, and not interferon induction genes, are evolving significantly more rapidly than a random set of genes. Interferon induction genes evolve in a way that is indistinguishable from a matched set of random genes (22% and 18% of genes bear signatures of positive selection, respectively). In contrast, interferon-stimulated genes evolve differently, with 33% of genes evolving under positive selection and containing a significantly higher fraction of codons that have experienced selection for recurrent replacement of the encoded amino acid. Conclusion Viruses may antagonize individual products of the interferon response more often than trying to neutralize the system altogether.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Farhan Quadir ◽  
Raj S. Roy ◽  
Randal Halfmann ◽  
Jianlin Cheng

AbstractDeep learning methods that achieved great success in predicting intrachain residue-residue contacts have been applied to predict interchain contacts between proteins. However, these methods require multiple sequence alignments (MSAs) of a pair of interacting proteins (dimers) as input, which are often difficult to obtain because there are not many known protein complexes available to generate MSAs of sufficient depth for a pair of proteins. In recognizing that multiple sequence alignments of a monomer that forms homomultimers contain the co-evolutionary signals of both intrachain and interchain residue pairs in contact, we applied DNCON2 (a deep learning-based protein intrachain residue-residue contact predictor) to predict both intrachain and interchain contacts for homomultimers using multiple sequence alignment (MSA) and other co-evolutionary features of a single monomer followed by discrimination of interchain and intrachain contacts according to the tertiary structure of the monomer. We name this tool DNCON2_Inter. Allowing true-positive predictions within two residue shifts, the best average precision was obtained for the Top-L/10 predictions of 22.9% for homodimers and 17.0% for higher-order homomultimers. In some instances, especially where interchain contact densities are high, DNCON2_Inter predicted interchain contacts with 100% precision. We also developed Con_Complex, a complex structure reconstruction tool that uses predicted contacts to produce the structure of the complex. Using Con_Complex, we show that the predicted contacts can be used to accurately construct the structure of some complexes. Our experiment demonstrates that monomeric multiple sequence alignments can be used with deep learning to predict interchain contacts of homomeric proteins.


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