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1.
Med J (Ft Sam Houst Tex) ; (PB 8-21-01/02/03): 12-19, 2021.
Article in English | MEDLINE | ID: mdl-33666906

ABSTRACT

BACKGROUND: COVID-19, caused by SARS CoV-2, is an acute respiratory viral illness. We present the experience of treating patients hospitalized with COVID-19 in a Role 3 hospital in an active warzone. METHODS: This is a retrospective care series of patients treated for COVID-19 at Craig Joint Theater Hospital, Bagram, Afghanistan from May to August 2020. Data extracted included demographics, admission and disposition information, past medical history, comorbidities, Transportation Command (TRANSCOM) severity classification (i.e. Category A, Category B), and treatments received. RESULTS: This series included 15 Category A and 55 Category B patients. Most patients were non-US contractors with one chronic condition. Most patients received medical treatments in accordance with Department of Defense Practice Management Guidelines. For Category A patients, mechanical ventilation use declined from a mean average of 10.67 days to 2.83 days following the introduction of high-flow nasal cannula. Average hospital length of stay was 6 days (range 2-23). One death occurred in a patient greater than 60 years old with three known prior medical conditions. Most patients were discharged to a non-medical isolation facility. Aeromedically evacuated patients were mostly US military and US contractors. CONCLUSION: We faced several challenges including retrofitting a Role 3 facility designed for trauma care for management of a highly contagious respiratory viral illness. Logistics constraints impacted timely delivery of medical therapies and equipment and decreased efficiency of aeromedical evacuation. Despite these challenges and the simultaneous trauma mission, most patients received medical care in accordance with treatment guidelines with a low mortality rate.


Subject(s)
COVID-19/therapy , Hospitalization , Hospitals, Military , Military Personnel , Adult , Afghanistan , Aged , COVID-19/diagnosis , COVID-19/mortality , Female , Humans , Male , Middle Aged , Retrospective Studies , Survival Rate , Treatment Outcome , United States
2.
J Bacteriol ; 190(17): 5972-80, 2008 Sep.
Article in English | MEDLINE | ID: mdl-18621903

ABSTRACT

Gram-negative bacteria display either a flat or an irregular outer membrane. The periodontal pathogen Aggregatibacter (Actinobacillus) actinomycetemcomitans has an irregular outer membrane. We have identified a gene that is associated with the biogenesis of this morphology. The gene is part of a three-gene operon and codes for a 141-kDa protein designated morphogenesis protein C (MorC), which is conserved in several gram-negative bacteria including Haemophilus influenzae and Pasteurella multocida. Insertional inactivation of this gene resulted in the conversion of an irregularly shaped membrane to a flat membrane. Associated with this morphological change were the autoaggregation of the bacteria during planktonic growth and a concomitant increase in the surface hydrophobicity of the bacterium. The absence of MorC also resulted in the loss of the secretion of leukotoxin but not the ltxA transcription. Our findings suggest that MorC is critical for membrane morphology and leukotoxin secretion in A. actinomycetemcomitans.


Subject(s)
Aggregatibacter actinomycetemcomitans/metabolism , Bacterial Proteins/metabolism , Exotoxins/metabolism , Membrane Proteins/metabolism , Aggregatibacter actinomycetemcomitans/genetics , Aggregatibacter actinomycetemcomitans/ultrastructure , Amino Acid Sequence , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Cell Membrane/metabolism , Cell Membrane/ultrastructure , Chromatography, Liquid , Electrophoresis, Polyacrylamide Gel , Hydrophobic and Hydrophilic Interactions , Immunoblotting , Membrane Proteins/chemistry , Membrane Proteins/genetics , Microscopy, Electron, Transmission , Molecular Sequence Data , Mutagenesis, Insertional , Operon/genetics , Promoter Regions, Genetic/genetics , Reverse Transcriptase Polymerase Chain Reaction , Sequence Homology, Amino Acid , Spectrometry, Mass, Electrospray Ionization
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