Letter to the Editor: Lack of Correlation between V3 Amino Acid Sequence and Syncytium-Inducing Capacity of Some HIV Type 1 Isolates

1996 ◽  
Vol 12 (10) ◽  
pp. 855-858 ◽  
Author(s):  
FARIDEH SABRI ◽  
FRANCESCA CHIODI ◽  
EVA MARIA FENYÖ
1995 ◽  
Vol 11 (5) ◽  
pp. 597-603 ◽  
Author(s):  
CAROL HOLM-HANSEN ◽  
DIETMAR GROTHUES ◽  
SIREN RUSTAD ◽  
BÅRD RØSOK ◽  
FLAVIA RODICA PASCU ◽  
...  

1999 ◽  
Vol 73 (5) ◽  
pp. 3975-3985 ◽  
Author(s):  
Cara C. Wilson ◽  
R. Clark Brown ◽  
Bette T. Korber ◽  
Barbara M. Wilkes ◽  
Debbie J. Ruhl ◽  
...  

ABSTRACT Host immunologic factors, including human immunodeficiency virus (HIV)-specific cytotoxic T lymphocytes (CTL), are thought to contribute to the control of HIV type 1 (HIV-1) replication and thus delay disease progression in infected individuals. Host immunologic factors are also likely to influence perinatal transmission of HIV-1 from infected mother to infant. In this study, the potential role of CTL in modulating HIV-1 transmission from mother to infant was examined in 11 HIV-1-infected mothers, 3 of whom transmitted virus to their offspring. Frequencies of HIV-1-specific human leukocyte antigen class I-restricted CTL responses and viral epitope amino acid sequence variation were determined in the mothers and their infected infants. Maternal HIV-1-specific CTL clones were derived from each of the HIV-1-infected pregnant women. Amino acid substitutions within the targeted CTL epitopes were more frequently identified in transmitting mothers than in nontransmitting mothers, and immune escape from CTL recognition was detected in all three transmitting mothers but in only one of eight nontransmitting mothers. The majority of viral sequences obtained from the HIV-1-infected infant blood samples were susceptible to maternal CTL. These findings demonstrate that epitope amino acid sequence variation and escape from CTL recognition occur more frequently in mothers that transmit HIV-1 to their infants than in those who do not. However, the transmitted virus can be a CTL susceptible form, suggesting inadequate in vivo immune control.


2009 ◽  
Vol 52 (3) ◽  
pp. 320-328 ◽  
Author(s):  
Piyamat Jinnopat ◽  
Panasda Isarangkura-na-ayuthaya ◽  
Piraporn Utachee ◽  
Yukiko Kitagawa ◽  
U Chandimal de Silva ◽  
...  

2004 ◽  
Vol 78 (7) ◽  
pp. 3722-3732 ◽  
Author(s):  
Lamei Chen ◽  
Alla Perlina ◽  
Christopher J. Lee

ABSTRACT Drug resistance is a major problem in the treatment of AIDS, due to the very high mutation rate of human immunodeficiency virus (HIV) and subsequent rapid development of resistance to new drugs. Identification of mutations associated with drug resistance is critical for both individualized treatment selection and new drug design. We have performed an automated mutation analysis of HIV Type 1 (HIV-1) protease and reverse transcriptase (RT) from approximately 40,000 AIDS patient plasma samples sequenced by Specialty Laboratories Inc. from 1999 to mid-2002. This data set provides a nearly complete mutagenesis of HIV protease and enables the calculation of statistically significant Ka /Ks values for each individual amino acid mutation in protease and RT. Positive selection (i.e., a Ka /Ks ratio of> 1, indicating increased reproductive fitness) detected 19 of 23 known drug-resistant mutation positions in protease and 20 of 34 such positions in RT. We also discovered 163 new amino acid mutations in HIV protease and RT that are strong candidates for drug resistance or fitness. Our results match available independent data on protease mutations associated with specific drug treatments and mutations with positive reproductive fitness, with high statistical significance (the P values for the observed matches to occur by random chance are 10−5.2 and 10−16.6, respectively). Our mutation analysis provides a valuable resource for AIDS research and will be available to academic researchers upon publication at http://www.bioinformatics.ucla.edu/HIV . Our data indicate that positive selection mapping is an analysis that can yield powerful insights from high-throughput sequencing of rapidly mutating pathogens.


2001 ◽  
Vol 183 (14) ◽  
pp. 4149-4156 ◽  
Author(s):  
Hirotaka Ichiki ◽  
Yoko Tanaka ◽  
Kiyotaka Mochizuki ◽  
Katsuhiko Yoshimatsu ◽  
Takeshi Sakurai ◽  
...  

ABSTRACT Cu-containing dissimilatory nitrite reductase (CuNiR) was purified from denitrifying cells of a halophilic archaeon, Haloarcula marismortui. The purified CuNiR appeared blue in the oxidized state, possessing absorption peaks at 600 and 465 nm in the visible region. Electron paramagnetic resonance spectroscopy suggested the presence of type 1 Cu (gII = 2.232; AII = 4.4 mT) and type 2 Cu centers (gII = 2.304; AII = 13.3 mT) in the enzyme. The enzyme contained two subunits, whose apparent molecular masses were 46 and 42 kDa, according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. N-terminal amino acid sequence analysis indicated that the two subunits were identical, except that the 46-kDa subunit was 16 amino acid residues longer than the 42-kDa subunit in the N-terminal region. A nirK gene encoding the CuNiR was cloned and sequenced, and the deduced amino acid sequence with a residual length of 361 amino acids was homologous (30 to 41%) with bacterial counterparts. Cu-liganding residues His-133, Cys-174, His-182, and Met-187 (for type 1 Cu) and His-138, His-173, and His-332 (for type 2 Cu) were conserved in the enzyme. As generally observed in the halobacterial enzymes, the enzymatic activity of the purified CuNiR was enhanced during increasing salt concentration and reached its maximum in the presence of 2 M NaCl with the value of 960 μM NO2 − · min−1 · mg−1.


1996 ◽  
Vol 12 (7) ◽  
pp. 565-566 ◽  
Author(s):  
Oliviero E. Varnier ◽  
Mauro Giacomini ◽  
Flavia B. Lillo

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