The depression of immune responses during measles infection has been recognized since the early 20th century. Acute bacterial infections are the most common cause of morbidity and mortality in measles. This study investigated the phagocytic and bactericidal or fungicidal capacities of polymorphonuclear cells (PMN) and monocytes during measles infections. When 14 children with measles were compared with 25 healthy controls, a significant depression in PMN and monocyte function was found. Of these 14 children, seven developed acute bacterial infections. These seven children were compared with 11 children who had acute bacterial infections without measles. It was found that PMN in patients with measles did not achieve an activated state, as expected with acute infections. Serum immunoglobulins were not altered in these patients. These results confirm previous reports of depressed phagocytic and bactericial capacities of PMN in measles, and further document that peripheral blood monocyte functions are also depressed in measles.
Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a significant public health problem in Southeast Asia. Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part of the heparin sulfate receptor binding region that drives the dengue virus (DENV)’s fusion with the host cell. Here, we used high-hydrostatic-pressure nuclear magnetic resonance (HHP-NMR) to obtain residue-specific information on the folding process of domain III from serotype 4 dengue virus (DEN4-ED3), which adopts the classical three-dimensional (3D) ß-sandwich structure known as the Ig-like fold. Interestingly, the folding pathway of DEN4-ED3 shares similarities with that of the Titin I27 module, which also adopts an Ig-like fold, but is functionally unrelated to ED3. For both proteins, the unfolding process starts by the disruption of the N- and C-terminal strands on one edge of the ß-sandwich, yielding a folding intermediate stable over a substantial pressure range (from 600 to 1000 bar). In contrast to this similarity, pressure-jump kinetics indicated that the folding transition state is considerably more hydrated in DEN4-ED3 than in Titin I27.
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