Molecular characterization of wild-type measles viruses in Tamil Nadu, India, during 2005-2006: Relationship of genotype D8 strains from Tamil Nadu to global strains

ABSTRACTThe prevalence of a genetic polymorphism(s) at codon 268 in the cytochromebgene, which is associated with failure of atovaquone-proguanil treatment, was analyzed in 227Plasmodium falciparumparasites from western Kenya. The prevalence of the wild-type allele was 63%, and that of the Y268S (denoting a Y-to-S change at position 268) mutant allele was 2%. There were no pure Y268C or Y268N mutant alleles, only mixtures of a mutant allele(s) with the wild type. There was a correlation between parasite 50% inhibitory concentration (IC50) and parasite genetic polymorphism; mutant alleles had higher IC50s than the wild type.

Download Full-text

Trans-splicing as a Novel Mechanism to Explain Interallelic Complementation in Drosophila

Genetics ◽

10.1093/genetics/160.4.1481 ◽

2002 ◽

Vol 160 (4) ◽

pp. 1481-1487 ◽

Cited By ~ 2

Author(s):

Fabien Mongelard ◽

Mariano Labrador ◽

Ellen M Baxter ◽

Tatiana I Gerasimova ◽

Victor G Corces

Keyword(s):

Molecular Characterization ◽

Wild Type ◽

Functional Protein ◽

Gypsy Insulator ◽

Type Function ◽

Homologous Chromosomes ◽

Trans Splicing ◽

Interallelic Complementation

AbstractTwo mutant alleles of the same gene, each located in one of the two homologous chromosomes, may in some instances restore the wild-type function of the gene. This is the case with certain combinations of mutant alleles in the mod(mdg4) gene. This gene encodes several different proteins, including Mod(mdg4)2.2, a component of the gypsy insulator. This protein is encoded by two separate transcription units that can be combined in a trans-splicing reaction to form the mature Mod(mdg4)2.2-encoding RNA. Molecular characterization of complementing alleles shows that they affect the two different transcription units. Flies homozygous for each allele are missing the Mod(mdg4)2.2 protein, whereas wild-type trans-heterozygotes are able to synthesize almost normal levels of the Mod(mdg4)2.2 product. This protein is functional as judged by its ability to form a functional insulator complex. The results suggest that the interallelic complementation in the mod(mdg4) gene is a consequence of trans-splicing between two different mutant transcripts. A conclusion from this observation is that the trans-splicing reaction that takes place between transcripts produced on two different mutant chromosomes ensures wild-type levels of functional protein.

Download Full-text

Molecular characterization of Helja, an extracellular jacalin-related protein from Helianthus annuus: Insights into the relationship of this protein with unconventionally secreted lectins

Journal of Plant Physiology ◽

10.1016/j.jplph.2015.06.004 ◽

2015 ◽

Vol 183 ◽

pp. 144-153 ◽

Cited By ~ 7

Author(s):

Marcela Pinedo ◽

Facundo Orts ◽

André de Oliveira Carvalho ◽

Mariana Regente ◽

Julia Ribeiro Soares ◽

...

Keyword(s):

Helianthus Annuus ◽

Molecular Characterization ◽

Related Protein ◽

Relationship Of ◽

The Relationship

Download Full-text

Molecular characterization of small and medium segments of Crimean-Congo hemorrhagic fever virus in Turkey

Future Virology ◽

10.2217/fvl-2020-0003 ◽

2020 ◽

Vol 15 (4) ◽

pp. 247-254

Author(s):

Murat Karamese ◽

Erkan Ozmen ◽

Hakan Aydin ◽

Mehmet Ozkan Timurkan ◽

Mesud Fakirullahoglu

Keyword(s):

Infectious Disease ◽

Phylogenetic Analysis ◽

Phylogenetic Tree ◽

Molecular Characterization ◽

Hemorrhagic Fever ◽

Fever Virus ◽

Crimean Congo Hemorrhagic Fever ◽

Hemorrhagic Fever Virus ◽

Relationship Of

Aim: The objective was to investigate the genotypic relationship of S and M segments in Crimean-Congo hemorrhagic fever virus (CCHFV) by phylogenetic analysis in 25 patients from seven endemic cities in Turkey. Materials & methods: A total of 25 samples from patients with CCHF were included between 2012 and 2015. Phylogenetic tree analyses were inferred using MEGA version-6.0 and distances were calculated by Kimura’s 2-parameter. Results: Phylogenetic analysis showed that all isolated viruses (n = 25) were in the predicted clades such as clade V- Europe-1 regarding both S and M segments of the CCHFV. Conclusion: Further epidemiological, molecular and phylogenic studies should be performed in both reservoir animals/vectors and humans to determine the incidence of tick-borne infectious disease and to help to develop vaccines for prevention of the disease.

Download Full-text

In Vitro Molecular Characterization of RNA–Proteins Interactions During Initiation of Translation of a Wild-Type and a Mutant Coxsackievirus B3 RNAs

Molecular Biotechnology ◽

10.1007/s12033-012-9592-x ◽

2012 ◽

Vol 54 (2) ◽

pp. 515-527 ◽

Cited By ~ 4

Author(s):

Amira Souii ◽

Manel Ben M’hadheb-Gharbi ◽

Mahjoub Aouni ◽

Jawhar Gharbi

Keyword(s):

Molecular Characterization ◽

Coxsackievirus B3 ◽

Wild Type ◽

Initiation Of Translation ◽

Proteins Interactions

Download Full-text

Inheritance and Molecular Characterization of a Novel Mutated AHAS Gene Responsible for the Resistance of AHAS-Inhibiting Herbicides in Rapeseed (Brassica napus L.)

International Journal of Molecular Sciences ◽

10.3390/ijms21041345 ◽

2020 ◽

Vol 21 (4) ◽

pp. 1345

Author(s):

Qianxin Huang ◽

Jinyang Lv ◽

Yanyan Sun ◽

Hongmei Wang ◽

Yuan Guo ◽

...

Keyword(s):

Brassica Napus ◽

Molecular Characterization ◽

Herbicide Resistance ◽

Acetohydroxyacid Synthase ◽

Cross Resistance ◽

Single Point Mutation ◽

Wild Type ◽

Brassica Napus L ◽

Herbicide Resistant

The use of herbicides is an effective and economic way to control weeds, but their availability for rapeseed is limited due to the shortage of herbicide-resistant cultivars in China. The single-point mutation in the acetohydroxyacid synthase (AHAS) gene can lead to AHAS-inhibiting herbicide resistance. In this study, the inheritance and molecular characterization of the tribenuron-methyl (TBM)-resistant rapeseed (Brassica napus L.) mutant, K5, are performed. Results indicated that TBM-resistance of K5 was controlled by one dominant allele at a single nuclear gene locus. The novel substitution of cytosine with thymine at position 544 in BnAHAS1 was identified in K5, leading to the alteration of proline with serine at position 182 in BnAHAS1. The TBM-resistance of K5 was approximately 100 times that of its wild-type ZS9, and K5 also showed cross-resistance to bensufuron-methyl and monosulfuron-ester sodium. The BnAHAS1544T transgenic Arabidopsis exhibited higher TBM-resistance than that of its wild-type, which confirmed that BnAHAS1544T was responsible for the herbicide resistance of K5. Simultaneously, an allele-specific marker was developed to quickly distinguish the heterozygous and homozygous mutated alleles BnAHAS1544T. In addition, a method for the fast screening of TBM-resistant plants at the cotyledon stage was developed. Our research identified and molecularly characterized one novel mutative AHAS allele in B. napus and laid a foundation for developing herbicide-resistant rapeseed cultivars.

Download Full-text

Molecular Characterization of Genes Coding for Wild-Type and Sulfonylurea-Resistant Acetolactate Synthase in the Cyanobacterium Synechococcus PC C7942

Zeitschrift für Naturforschung C ◽

10.1515/znc-1990-0541 ◽

1990 ◽

Vol 45 (5) ◽

pp. 538-543 ◽

Cited By ~ 6

Author(s):

D. Friedberg ◽

J. Seijffers

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequence ◽

Molecular Characterization ◽

Amino Acid Level ◽

Acetolactate Synthase ◽

Mutant Gene ◽

Wild Type ◽

E Coli

We present here the isolation and molecular characterization of acetolactate synthase (ALS) genes from the cyanobacterium Synechococcus PCC7942 which specify a sulfonylurea-sensitive enzyme and from the sulfonylurea-resistant mutant SM3/20, which specify resistance to sulfonylurea herbicides. The ALS gene was cloned and mapped by complementation of an Escherichia coli ilv auxotroph that requires branched-chain amino acids for growth and lacks ALS activity. The cyanobacterial gene is efficiently expressed in this heterologous host. The ALS gene codes for 612 amino acids and shows high sequence homology (46%) at the amino acid level with ALS III of E. coli and with the tobacco ALS. The resistant phenotype is a consequence of proline to serine substitution in residue 115 of the deduced amino acid sequence. Functional expression of the mutant gene in wild-type Synechococcus and in E. coli confirmed that this amino-acid substitution is responsible for the resistance. Yet the deduced amino-acid sequence as compared with othjer ALS proteins supports the notion that the amino-acid context of the substitution is important for the resistance.

Download Full-text