Characterization of a new HLA-G allele encoding a nonconservative amino acid substitution in the α3 domain (exon 4) and its relevance to certain complications in pregnancy

2001 ◽  
Vol 53 (1) ◽  
pp. 48-53 ◽  
Author(s):  
Thomas Vauvert F. Hviid ◽  
Ole B. Christiansen ◽  
Jørgen Krogh Johansen ◽  
Ulla Römmelmayer Hviid ◽  
Claus Lundegaard ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Exon 4 ◽  
Domain Exon ◽  
In Pregnancy

scholarly journals Diversity of TEM Mutants in Proteus mirabilis

1999 ◽  
Vol 43 (11) ◽  
pp. 2671-2677 ◽  
Author(s):  
R. Bonnet ◽  
C. De Champs ◽  
D. Sirot ◽  
C. Chanal ◽  
R. Labia ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Proteus Mirabilis ◽  
Clinical Isolates ◽  
Amino Acid Substitutions ◽  
First Report ◽  
Conjugative Plasmids ◽  
Extended Spectrum ◽  
Nucleotide Mutation

ABSTRACT In a survey of resistance to amoxicillin among clinical isolates ofProteus mirabilis, 10 TEM-type β-lactamases were characterized: (i) the well-known penicillinases TEM-1 and TEM-2, the extended-spectrum β-lactamases (ESBLs) TEM-3 and TEM-24, and the inhibitor-resistant TEM (IRT) TEM-44 and (ii) five novel enzymes, a penicillinase TEM-57 similar to TEM-1, an ESBL TEM-66 similar to TEM-3, and three IRTs, TEM-65, TEM-73, and TEM-74. The penicillinase TEM-57 and the ESBL TEM-66 differed from TEM-1 and TEM-3, respectively, by the amino acid substitution Gly-92→Asp (nucleotide mutation G-477→A). This substitution could have accounted for the decrease in pIs (5.2 for TEM-57 and 6.0 for TEM-66) but did not necessarily affect the intrinsic activities of these enzymes. The IRT TEM-65 was an IRT-1-like IRT (Cys-244) related to TEM-2 (Lys-39). The two other IRTs, TEM-73 and TEM-74, were related to IRT-1 (Cys-244) and IRT-2 (Ser-244), respectively, and harbored the amino acid substitutions Leu-21→Phe and Thr-265→Met. In this study, the ESBLs TEM-66, TEM-24, and TEM-3 were encoded by large (170- to 180-kb) conjugative plasmids that exhibited similar patterns after digestion and hybridization with the TEM and AAC(6′)I probes. The three IRTs TEM-65, TEM-73, and TEM-74 were encoded by plasmids that ranged in size from 42 to 70 kb but for which no transfer was obtained. The characterization of five new plasmid-mediated TEM-type β-lactamases and the first report of TEM-24 in P. mirabilis are evidence of the wide diversity of β-lactamases produced in this species and of its possible role as a β-lactamase-encoding plasmid reservoir.

Molecular characterization of lactoferrin gene and its association with mastitis in crossbred cattle

2015 ◽  
Vol 49 (6) ◽  
Author(s):  
Vaibhav Patel ◽  
Bharat Bhushan ◽  
Vishnu Kumar ◽  
Manjit Panigrahi ◽  
Sanjeev Ranjan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Genomic Dna ◽  
Least Square ◽  
Crossbred Cattle ◽  
Cloning And Sequencing ◽  
Brown Swiss ◽  
Lactoferrin Gene ◽  
Exon 4

Genomic DNA was isolated from the blood of 100 crossbred cattle (HF, Jersey, Brown Swiss x Hariana cattle). Exon 4 and intron 6 of lactoferrin (Lf) gene was characterized by PCR-SSCP. Two alleles of exon 4, namely E & F showing two genotypes EE and EF and two alleles of intron 6, namely A and B showing two genotypes AA and AB were found in studied population. Cloning and sequencing results revealed that in exon 4, there was one SNP in allele E and two SNPs in allele F, which changed amino acid isoleucine to valine. In intron 6 there was one SNP in allele A and three SNPs in allele B. Least square analysis for SCC and FLMY revealed that genotype AA was significantly associated with low SCC, while genotype AB was significantly associated with high SCC. However, genotype EE was significantly associated with FLMY as compared to genotype EF.

Characterization of the mouse thyrotrophin-releasing hormone receptor gene: an exon corresponds to a deletion in the rat cDNA

1993 ◽  
Vol 11 (2) ◽  
pp. 141-149 ◽  
Author(s):  
S M Duthie ◽  
P L Taylor ◽  
K A Eidne
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Stop Codon ◽  
Amino Acid Sequences ◽  
R Gene ◽  
Coding Region ◽  
Thyrotrophin Releasing Hormone ◽  
Exon 2 ◽  
Exon 4

ABSTRACT The cloning and characterization of the mouse TRH receptor (TRH-R) gene revealed an untranslated exon (exon 1), a single intron and an upstream dinucleotide repeat sequence (d(TG)16.d(AG)21) in the 5′ untranslated region (UTR). The coding region was contained almost entirely on a second exon (exon 2), with the final amino acid and stop codon at the COOH terminus of the gene encoded by a third exon (exon 3) flanked by two introns. The 3′ UTR was contained on the remainder of exon 3 and on the final exon (exon 4). Exon 3 (228 bp) corresponds exactly to a 228 bp deletion that exists in the rat TRH-R cDNA, but not in the mouse cDNA. The mouse TRH-R cDNA encodes a protein of 393 amino acids which is 96% homologous to the rat TRH-R protein of 412 amino acids, but is 19 amino acids shorter at its COOH terminus. The coding sequence for these 19 amino acids (plus 1 extra amino acid) does exist in the mouse TRH-R gene, but the sequence is encoded by exon 4, separated from the rest of the coding region by the stop codon and 223 bp of 3′ UTR on exon 3. Splicing of exon 3 in the mouse TRH-R gene would remove the last amino acid, the stop codon and the 223 bp of 3′ UTR, allowing transcription to continue into the 3′ UTR on exon 4, which encodes the 19 extra amino acids found in the rat cDNA. This would then result in an alternative 412 amino acid version of the mouse TRH-R protein, with 95% homology to the rat TRH-R. This study focused on the structural differences in the intracellular COOH-terminal tail of the receptor, which is known to be a functionally important domain in other members of the G protein-coupled receptor family. We have also recently characterized the human TRH-R cDNA, which revealed a third variant at the COOH terminus. Comparisons between mouse, rat and human TRH-Rs show that the amino acid sequences are virtually identical. However, significant differences between these species exist at the COOH terminus, with each TRH-R having a unique form of the COOH-terminal tail, beginning at exactly the same site and encoding 1, 20 and 6 amino acids in the mouse, rat and human respectively.

scholarly journals Characterization of Nocardithiocin Derivatives Produced by Amino Acid Substitution of Precursor Peptide notG

2019 ◽  
Vol 26 (1) ◽  
pp. 281-290 ◽  
Author(s):  
Kanae Sakai ◽  
Yasumasa Hara ◽  
Masami Ishibashi ◽  
Mai Sakai ◽  
Seiya Kawahara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Precursor Peptide

Hb VILA REAL [β36(C2)Pro → His] IN ITALY: CHARACTERIZATION OF THE AMINO ACID SUBSTITUTION AND THE DNA MUTATION

Hemoglobin ◽  
2002 ◽  
Vol 26 (1) ◽  
pp. 21-31 ◽  
Author(s):  
Anna Maria Salzano ◽  
Virginia Carbone ◽  
Leonilde Pagano ◽  
Salvatore Buffardi ◽  
Carlo De Rosa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Dna Mutation

scholarly journals Molecular Characterization of rpoBMutations Conferring Cross-Resistance to Rifamycins on Methicillin-Resistant Staphylococcus aureus

1999 ◽  
Vol 43 (11) ◽  
pp. 2813-2816 ◽  
Author(s):  
Thomas A. Wichelhaus ◽  
Volker Schäfer ◽  
Volker Brade ◽  
Boris Böddinghaus
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Molecular Characterization ◽  
Amino Acid Substitution ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Cross Resistance ◽  
Methicillin Resistant ◽  
Low Level ◽  
Level Resistance

ABSTRACT Mutations of the rpoB gene conferring resistance to rifampin were analyzed in 40 methicillin-resistant Staphylococcus aureus isolates obtained from six countries. Interestingly, the majority of clinical isolates showed multiple mutations withinrpoB. The amino acid substitution 481His→Asn was the most prevalent one, capable of conferring low-level resistance on its own. Cross-resistance to rifampin, rifabutin, and rifapentine was demonstrated for all mutants identified. The level of resistance to rifamycins correlated with both the mutation position and type of amino acid substitution.

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