Characterization of alternative amino acid substitutions at arginine 830 of the androgen receptor that cause complete androgen insensitivity in three families

We characterized eleven H9N2 influenza A viruses isolated from chicken products imported from China. Genetically they were classified into six distinct genotypes, including five already known genotypes and one novel genotype. This suggested that such multiple genotypes of the H9N2 virus have possibly already become widespread and endemic in China. Two isolates have amino-acid substitutions that confer resistance to amantadine in the M2 region, and this supported the evidence that this mutation might be a result of the wide application of amantadine for avian influenza treatment in China. These findings emphasize the importance of surveillance for avian influenza virus in this region, and of quarantining imported chicken products as potential sources for the introduction of influenza virus.

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Molecular characterization of a 13-amino acid deletion in VP1 (1D) protein and novel amino acid substitutions in 3D polymerase protein of foot and mouth disease virus subtype A/Iran87

Journal of Veterinary Science ◽

10.4142/jvs.2011.12.4.363 ◽

2011 ◽

Vol 12 (4) ◽

pp. 363 ◽

Cited By ~ 2

Author(s):

Majid Esmaelizad ◽

Saber Jelokhani-Niaraki ◽

Khadije Hashemnejad ◽

Morteza Kamalzadeh ◽

Mohsen Lotfi

Keyword(s):

Amino Acid ◽

Molecular Characterization ◽

Disease Virus ◽

Foot And Mouth Disease ◽

Amino Acid Substitutions ◽

Amino Acid Deletion ◽

Mouth Disease Virus ◽

Subtype A ◽

Virus Subtype

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Pathophysiology of Androgen Insensitivity Syndromes: Molecular and Structural Approaches of Natural and Engineered Androgen Receptor Mutations at Amino Acid 743

The Journal of Clinical Endocrinology & Metabolism ◽

10.1210/jc.2002-020491 ◽

2002 ◽

Vol 87 (12) ◽

pp. 5793-5800 ◽

Cited By ~ 6

Author(s):

Nicolas Poujol ◽

Serge Lumbroso ◽

Béatrice Térouanne ◽

Jean-Marc A. Lobaccaro ◽

William Bourguet ◽

...

Keyword(s):

Androgen Receptor ◽

Amino Acid ◽

Androgen Insensitivity

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Single amino acid substitution (840Arg → His) in the hormone-binding domain of the androgen receptor leads to incomplete androgen insensitivity syndrome associated with a thermolabile androgen receptor

Acta Endocrinologica ◽

10.1530/eje.0.1300569 ◽

1994 ◽

Vol 130 (6) ◽

pp. 569-574 ◽

Cited By ~ 19

Author(s):

Kyosuke Imasaki ◽

Tomonobu Hasegawa ◽

Taijiro Okabe ◽

Yoshiyuki Sakai ◽

Masafumi Haji ◽

...

Keyword(s):

Androgen Receptor ◽

Amino Acid ◽

Amino Acid Substitution ◽

Androgen Insensitivity Syndrome ◽

Binding Domain ◽

Single Amino Acid Substitution ◽

Single Amino Acid ◽

Hormone Binding ◽

Androgen Insensitivity ◽

Hormone Binding Domain

Imasaki K, Hasegawa T. Okabe T. Sakai Y. Haji M. Takayanagi R, Nawata H. Single amino acid substitution (840Arg → His) in the hormone-binding domain of the androgen receptor leads to incomplete androgen insensitivity syndrome associated with a thermolabile androgen receptor. Eur I Endocrinol 1994;130:569–74. ISSN 0804–4643 We have characterized the androgen receptor in a Japanese girl and her maternal cousin in a family with incomplete androgen insensitivity syndrome, and have investigated the molecular basis. Wholecell androgen binding assay in cultured genital skin fibroblasts from both patients showed a normal maximum binding capacity and a normal apparent dissociation constant. However, androgen binding in fibroblasts from both patients decreased to 30% when the assay temperature was raised from 30°C to 41°C, indicating the presence of the thermolability of ligand binding to the androgen receptor. Sequence analysis of the coding exons of the androgen receptor gene from the patients revealed a single nucleotide substitution at position 2881 in exon G, resulting in the conversion of arginine (CGT) to histidine (CAT) at amino acid position 840 in the hormone-binding domain of the androgen receptor. The family study showed that the mothers and the maternal grandmother of the patients are heterozygous carriers for this mutation, whereas the father does not carry it, supporting the view that androgen insensitivity syndrome is an X chromosome-linked disorder. The single amino acid substitution may explain the qualitative abnormality of the androgen receptor displaying thermolability, which is thought to be the pathogenesis of incomplete androgen insensitivity syndrome in the patients. Kyosuke Imasaki, Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812, Japan

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Characterization of amino acid substitutions in feline coronavirus 3C-like protease from a cat with feline infectious peritonitis treated with a protease inhibitor

Veterinary Microbiology ◽

10.1016/j.vetmic.2019.108398 ◽

2019 ◽

Vol 237 ◽

pp. 108398 ◽

Cited By ~ 7

Author(s):

Krishani Dinali Perera ◽

Athri D. Rathnayake ◽

Hongwei Liu ◽

Niels C. Pedersen ◽

William C. Groutas ◽

...

Keyword(s):

Amino Acid ◽

Protease Inhibitor ◽

Amino Acid Substitutions ◽

Feline Infectious Peritonitis ◽

Feline Coronavirus

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Characterization of Amino Acid Substitutions in the Putative Binding Site of Bupropion in Glic

Biophysical Journal ◽

10.1016/j.bpj.2019.11.3162 ◽

2020 ◽

Vol 118 (3) ◽

pp. 583a

Author(s):

Dubem Onyejegbu ◽

Jessica Shepherd ◽

Elham Pirayesh ◽

Akash Pandhare ◽

Zackary R. Gallardo ◽

...

Keyword(s):

Amino Acid ◽

Binding Site ◽

Amino Acid Substitutions ◽

Putative Binding Site

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Diversity of TEM Mutants in Proteus mirabilis

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.43.11.2671 ◽

1999 ◽

Vol 43 (11) ◽

pp. 2671-2677 ◽

Cited By ~ 51

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.

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