Unveiling molecular mechanisms of pneumococcal surface protein A interactions with antibodies and lactoferrin
Abstract
Streptococcus pneumoniae is a Gram-positive bacterium and a major human pathogen. The organism displays on its surface a variety of molecules that are involved in many essential processes including interactions with the tissues and molecules of its human host. A number of such surface molecules are essential virulence factors in disease processes and pathogenesis during all stages of bacterial life. Here we introduce one such surface protein, pneumococcal surface protein A (PspA), and show its molecular and structural aspects, and underlying mechanism of function at the atomic level as currently understood. The basis of its anti-complementary properties and functional interactions with its ligand, lactoferrin, is discussed. The PspA antigen binding to lactoferrin prevents the bactericidal effect of this human molecule of many functions. This review is focused on new function characterization studies performed during this century (year 2001 and later). Earlier studies on PspA were reviewed by this author in 2001 and 2004 [Jedrzejas MJ. Pneumococcal virulence factors: structure and function. Microbiol Mol Biol Rev, 2001;65:187-207; Jedrzejas MJ. Extracellular virulence factors of Streptococcus pneumoniae. Front Biosci 2004;9:891-...Continue Reading
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