scholarly journals Update and nomenclature proposal for mammalian lysophospholipid acyltransferases which create membrane phospholipid diversity

2021 ◽  
pp. 101470
Author(s):  
William J. Valentine ◽  
Keisuke Yanagida ◽  
Hiroki Kawana ◽  
Nozomu Kono ◽  
Nobuo N. Noda ◽  
...  
Author(s):  
Daniel J Wolter ◽  
Alison Scott ◽  
Catherine R Armbruster ◽  
Dale Whittington ◽  
John S Edgar ◽  
...  

Abstract Background Bacteria adapt to survive and grow in different environments. Genetic mutations that promote bacterial survival under harsh conditions can also restrict growth. The causes and consequences of these adaptations have important implications for diagnosis, pathogenesis, and therapy. Objectives We describe the isolation and characterization of an antibiotic-dependent, temperature-sensitive Pseudomonas aeruginosa mutant chronically infecting the respiratory tract of a cystic fibrosis (CF) patient, underscoring the clinical challenges bacterial adaptations can present. Methods Respiratory samples collected from a CF patient during routine care were cultured for standard pathogens. P. aeruginosa isolates recovered from samples were analysed for in vitro growth characteristics, antibiotic susceptibility, clonality, and membrane phospholipid and lipid A composition. Genetic mutations were identified by whole genome sequencing. Results P. aeruginosa isolates collected over 5 years from respiratory samples of a CF patient frequently harboured a mutation in phosphatidylserine decarboxylase (psd), encoding an enzyme responsible for phospholipid synthesis. This mutant could only grow at 37°C when in the presence of supplemented magnesium, glycerol, or, surprisingly, the antibiotic sulfamethoxazole, which the source patient had repeatedly received. Of concern, this mutant was not detectable on standard selective medium at 37°C. This growth defect correlated with alterations in membrane phospholipid and lipid A content. Conclusions A P. aeruginosa mutant chronically infecting a CF patient exhibited dependence on sulphonamides and would likely evade detection using standard clinical laboratory methods. The diagnostic and therapeutic challenges presented by this mutant highlight the complex interplay between bacterial adaptation, antibiotics, and laboratory practices, during chronic bacterial infections.


2002 ◽  
Vol 23 (4) ◽  
pp. 547-553 ◽  
Author(s):  
Robert A Sweet ◽  
Kanagasabai Panchalingam ◽  
Jay W Pettegrew ◽  
Richard J McClure ◽  
Ronald L Hamilton ◽  
...  

2001 ◽  
Vol 108 (8-9) ◽  
pp. 1081-1091 ◽  
Author(s):  
A. Schmitt ◽  
A. Maras ◽  
G. Petroianu ◽  
D. F. Braus ◽  
L. Scheuer ◽  
...  

1994 ◽  
Vol 124 (3) ◽  
pp. 273-287 ◽  
Author(s):  
TP McGee ◽  
HB Skinner ◽  
EA Whitters ◽  
SA Henry ◽  
VA Bankaitis

SEC14p is required for protein transport from the yeast Golgi complex. We describe a quantitative analysis of yeast bulk membrane and Golgi membrane phospholipid composition under conditions where Golgi secretory function has been uncoupled from its usual SEC14p requirement. The data demonstrate that SEC14p specifically functions to maintain a reduced phosphatidylcholine content in Golgi membranes and indicate that overproduction of SEC14p markedly reduces the apparent rate of phosphatidylcholine biosynthesis via the CDP-choline pathway in vivo. We suggest that SEC14p serves as a sensor of Golgi membrane phospholipid composition through which the activity of the CDP-choline pathway in Golgi membranes is regulated such that a phosphatidylcholine content that is compatible with the essential secretory function of these membranes is maintained.


2014 ◽  
Vol 146 (5) ◽  
pp. S-568 ◽  
Author(s):  
Samara Rifkin ◽  
Martha J. Shrubsole ◽  
Qiuyin Cai ◽  
Walter E. Smalley ◽  
Reid Ness ◽  
...  

Biochemistry ◽  
1997 ◽  
Vol 36 (22) ◽  
pp. 6768-6776 ◽  
Author(s):  
Kitty de Jong ◽  
Danielle Geldwerth ◽  
Frans A. Kuypers

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