Biswas G D, Anderson J E, Chen C J, Cornelissen C N, Sparling P F
Department of Medicine, School of Medicine, University of North Carolina at Chapel Hill 27599, USA.
Infect Immun. 1999 Jan;67(1):455-9. doi: 10.1128/IAI.67.1.455-459.1999.
We cloned lbpB, encoding a predicted 80-kDa lipoprotein, upstream of lbpA. A nonpolar mutant (LbpB- LbpA+) had normal lactoferrin (LF) binding and grew normally with LF as an iron source, whereas LbpB- LbpA- and LbpB+ LbpA- strains had reduced binding of LF and did not grow with LF as an iron source. LbpB bound LF directly in an affinity purification, suggesting that LbpB might play a still-uncharacterized role in the LF iron utilization.
我们在lbpA上游克隆了编码预测分子量为80 kDa脂蛋白的lbpB。一个非极性突变体(LbpB - LbpA +)具有正常的乳铁蛋白(LF)结合能力,并且以LF作为铁源时生长正常,而LbpB - LbpA - 和LbpB + LbpA - 菌株对LF的结合减少,并且不能以LF作为铁源生长。在亲和纯化中,LbpB直接结合LF,这表明LbpB可能在LF铁利用中发挥尚未明确的作用。