ABSTRACT
Self-contained underwater breathing apparatus (SCUBA) diving is an ever-growing sport, and despite a myriad of technological advances to improve safety, it remains dangerous. Providers of medical care for SCUBA divers must have an understanding of diving physiology and potential medical problems that can occur. SCUBA diving also can take participants to remote areas, so being properly prepared for potential emergencies can make a significant difference. The following is a review of diving physiology and the medical problems that can occur in SCUBA divers, along with some suggestions as to how to prepare for a SCUBA excursion.
Subject(s)
Diving/adverse effects , Diving/physiology , Animals , Barotrauma/etiology , Bites and Stings/diagnosis , Bites and Stings/therapy , Cnidarian Venoms/adverse effects , Decompression Sickness/diagnosis , Decompression Sickness/etiology , Decompression Sickness/therapy , Ear, Middle/injuries , Embolism, Air/diagnosis , Embolism, Air/etiology , Embolism, Air/therapy , Frontal Sinus/injuries , Humans , Lung Injury/etiology , Maxillary Sinus/injuries , Medical History Taking , Physical Examination , Pneumothorax/etiologyABSTRACT
Genomic RNA of primate lentiviruses serves both as an mRNA that encodes Gag and Gag-Pol polyproteins and as a propagated genome. Translation of this RNA is initiated by standard cap dependant mechanism or by internal entry of the ribosome. Two regions of the genomic RNA are able to attract initiation complexes, the 5' untranslated region and the gag coding region itself. Relying on probing data and a phylogenetic study, we have modelled the secondary structure of HIV-1, HIV-2 and SIV(Mac) coding region. This approach brings to light conserved secondary-structure elements that were shown by mutations to be required for internal entry of the ribosome. No structural homologies with other described viral or cellular IRES can be identified and lentiviral IRESes show many peculiar properties. Most notably, the IRES present in HIV-2 gag coding region is endowed with the unique ability to recruit up to three initiation complexes on a single RNA molecule. The structural and functional properties of gag coding sequence define a new type of IRES. Although its precise role is unknown, the conservation of the IRES among fast evolving lentiviruses suggests an important physiological role.
Subject(s)
HIV-2/genetics , Peptide Chain Initiation, Translational , RNA, Viral/chemistry , gag Gene Products, Human Immunodeficiency Virus/genetics , Ecthyma, Contagious , Eukaryotic Initiation Factors/metabolism , Genome, Viral , HIV-1/genetics , Mutagenesis, Site-Directed , Nucleic Acid Conformation , RNA, Viral/metabolism , Simian Immunodeficiency Virus/geneticsABSTRACT
The 5' untranslated region (5'UTR) of lentiviral genomic RNA is highly structured, and is the site of multiple RNA-RNA and RNA-protein interactions throughout the viral life cycle. The 5'UTR plays a critical role during transcription, translational regulation, genome dimerization, reverse transcription priming and encapsidation. The 5'UTR structures of human lentiviruses have been extensively studied, yet the respective role and conformation of each domain is still controversial. To gain insight into the structure-function relationship of lentiviral 5'UTRs, we modelled the RNA structure of the feline immunodeficiency virus (FIV), a virus that is evolutionarily distant from the primate viruses. Through combined chemical and enzymatic structure probing and a thorough phylogenetic study, we establish a model for the secondary structure of the 5'UTR and Gag coding region. This work highlights properties common to all lentiviruses, like the primer binding site structure and the presence of a stable stem-loop at the 5' extremity. We find that FIV has also evolved specific features, including a long stem loop overlapping the end of the 5'UTR and the beginning of the coding region. In addition, we observed footprints of Gag protein on each side of the initiation codon, this sheds light on the role of the sequences required for encapsidation.
