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, the etiological agent of periodontal disease, is an anaerobe that requires iron in the form of heme for growth. This chapter discusses the roles of specific outer membrane proteins and gingipains in heme accumulation by . The binding and accumulation of hemoglobin by is currently the focus of investigations being conducted in several independent laboratories. Recent investigations have indicated a significant role for the gingipain proteases in the acquisition of heme from hemoglobin. The gingipains of specifically cleave substrates behind either arginine or lysine residues. In addition to gingipains, hemagglutinins may aid in iron-heme utilization in . Due to the obligate requirement for iron by the expression of specific iron uptake systems is an important survival mechanism. The development of effective control strategies for infection requires an understanding of the iron transport systems required for in vivo growth of this organism. does not produce siderophores as do many other pathogens. Recent investigations of the acquisition of heme by have led to the identification of several outer membrane receptors. While the function of many of these putative receptors remains to be determined by mutational analysis, the initial analyses have provided the primary insight into how acquires heme. The involvement of the gingipains, particularly Kgp, indicates that in addition to specific outer membrane proteins, may use a hemophorelike delivery system.

Citation: Genco C, Simpson W, Olczak T. 2004. , p 329-343. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch21

Key Concept Ranking

Outer Membrane Proteins
Enzyme-Linked Immunosorbent Assay
Gene Expression and Regulation
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Image of FIGURE 1

Structures of gingipains HRgpA and Kgp. The sizes of the hemagglutinin domains (HA1 to HA4) are indicated. Amino acids involved in posttranslational processing are indicated by arrows. Areas of similar shading indicate sequences identical in both proteins. Percentages represent the degree of identity between the two compared regions of HRgpA and Kgp.

Citation: Genco C, Simpson W, Olczak T. 2004. , p 329-343. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch21
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Image of FIGURE 2

Three proposed mechanisms of heme transport in . (A) The degradation of a red blood cell (RBC) by a hemolysin liberates hemoglobin (Hb) and possibly heme. These iron sources may bind directly to HmuR working in cooperation with the putative TonB, ExbB, and ExbD proteins. (B) Soluble Kgp, acting as a hemophore-like protein, binds free hemoglobin and delivers it to HmuR. Either Kgp or hemoglobin may directly interact with HmuR. (C) Membrane-bound Kgp degrades hemoglobin, liberating free heme. This free heme may bind to HmuR or to a separate heme receptor (HmR). In all three scenarios, the transport of heme into the cytoplasm is facilitated by the use of a cytoplasmic membrane-bound permease working in cooperation with an ATPase. Once internalized, a putative degradative protein, such as heme oxygenase, may degrade heme.

Citation: Genco C, Simpson W, Olczak T. 2004. , p 329-343. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch21
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Generic image for table

Heme-binding proteins identified in

Citation: Genco C, Simpson W, Olczak T. 2004. , p 329-343. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch21

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