CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5

Article Abstract:

The affinity of the interaction between the chemokine receptor CCR-5 and the human immunodeficiency viruses type 1 (HIV-1) gp120 glycoproteins is higher in the presence of the primary receptor CD4. The interaction inhibits the high-affinity binding site of the macrophage inflammatory protein (MIP)-1-alpha and MIP-1-beta. The glycoproteins rearrange themselves during the entry of HIV-1 into the target cells to maximize CCR-5 binding. The absence of the gp120 glycoproteins also leads to an interaction between the two-domain D1 and D2 CD4 fragments and the CCR-5.

Glycoproteins, CD4 lymphocytes, HIV antibodies

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The C5a chemoattractant receptor mediates mucosal defence to infection

Article Abstract:

The C5a chemoattractant receptor is involved in a non-redundant function of mucosal host defence from lung infection. Mice deficient in C5a receptor are unable to clear intrapulmonary-instilled Pseudomonas aeruginosa and die of pneumonia. The mice are unable to clear the bacteria in spite of a significant increase in neutrophil influx. When challenged with sublethal inocula of Pseudomonas, these mice become superinfected with secondary bacterial strains. However, the C5a receptor is redundant in the peritoneum.

Observations, Natural immunity, Nasal mucosa

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Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor

Article Abstract:

Binding of bacterial phosphorylcholine to the platelet-activating factor (PAF) receptor increases the adherence of Streptococcus pneumoniae to human cells which is negated by PAF-receptor-mediated antagonists. Inflammatory activation of cells transfers the targeting of pneumococcus cells to a novel G-protein-coupled PAF receptor. The physiological relevance of the pneumococcal-PAF receptor interaction is discussed.

Blood platelets, Streptococcus pneumoniae, Platelet-derived growth factor receptors, Platelet activating factor

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