Neonatal mortality in a referral hospital in Cameroon over a seven year period: trends, associated factors and causes.

Background: The fourth Millennium Development Goals targets reduction by 2/3 the mortality rate of under-fives by 2015. This reduction starts with that of neonatal mortality representing 40% of childhood mortality. In Cameroon neonatal mortality was 31‰ in 2011.Objectives: We assessed the trends, associated factors and causes of neonatal deaths at the Yaounde Gynaeco-Obstetric and Pediatric Hospital.Methods: The study was a retrospective chart review. Data was collected from the hospital records, and included both maternal and neonatal variables from 1st January 2004 to 31st December 2010.Results: The neonatal mortality was 10%. Out-borns represented 49.3% of the deceased neonates with 11.3% born at home. The neonatal mortality rate followed a downward trend dropping from12.4% in 2004 to 7.2% in 2010. The major causes of deaths were: neonatal sepsis (37.85%), prematurity (31.26%), birth asphyxia (16%), and congenital malformations (10.54%). Most (74.2%) of the deaths occurred within the first week with 35% occurring within 24hours of life. Mortality was higher in neonates with birth weight less than 2500g and a gestational age of less than 37 weeks. In the mothers, it was high in single parenthood , primiparous and in housewives and students.Conclusion: There has been a steady decline of neonatal mortality since 2004. Neonatal sepsis, prematurity, birth asphyxia and congenital malformations were the major causes of neonatal deaths. Neonatal sepsis remained constant although at lower rates over the study period.Key words: mortality, neonates, referral hospital, Cameroo

Methanobactin and the Link Between Copper and Bacterial Methane Oxidation

Methanobactins (mbs) are low-molecular-mass (<1,200 Da) copper-binding peptides, or chalkophores, produced by many methane-oxidizing bacteria (methanotrophs). These molecules exhibit similarities to certain iron-binding siderophores but are expressed and secreted in response to copper limitation. Structurally, mbs are characterized by a pair of heterocyclic rings with associated thioamide groups that form the copper coordination site. One of the rings is always an oxazolone and the second ring an oxazolone, an imidazolone, or a pyrazinedione moiety. The mb molecule originates from a peptide precursor that undergoes a series of posttranslational modifications, including (i) ring formation, (ii) cleavage of a leader peptide sequence, and (iii) in some cases, addition of a sulfate group. Functionally, mbs represent the extracellular component of a copper acquisition system. Consistent with this role in copper acquisition, mbs have a high affinity for copper ions. Following binding, mbs rapidly reduce Cu2+ to Cu1+. In addition to binding copper, mbs will bind most transition metals and near-transition metals and protect the host methanotroph as well as other bacteria from toxic metals. Several other physiological functions have been assigned to mbs, based primarily on their redox and metal-binding properties. In this review, we examine the current state of knowledge of this novel type of metal-binding peptide. We also explore its potential applications, how mbs may alter the bioavailability of multiple metals, and the many roles mbs may play in the physiology of methanotrophs