Humoral responses to Porphyromonas gingivalis gingipain adhesin domains in subjects with chronic periodontitis.
Humoral responses to Porphyromonas gingivalis gingipain adhesin domains in subjects with chronic periodontitis.
复制标题
慢性牙周炎受试者对牙龈卟啉单胞菌牙龈蛋白酶粘附素结构域的体液反应。
DOI：
10.1128/iai.72.3.1374-1382.2004
复制
发表时间：
2004
影响因子：
3.1
通讯作者：
Hunter,Neil
中科院分区：
文献类型：
--
作者：
Nguyen,Ky-Anh;DeCarlo,ArthurA;Paramaesvaran,Mayuri;Collyer,CharlesA;Langley,DavidB;Hunter,Neil
The gingipains have been implicated in the pathogenicity ofPorphyromonas gingivalis, a major etiologic agent of chronic periodontitis. Mature gingipains often present as a membrane-bound glycosylated proteinase-adhesin complex comprising multiple adhesin domains (HA1 to -4) and a catalytic domain. Using recombinant adhesin domains, we were able to show that patients with chronic periodontitis produce significantly more immunoglobulin G reactive with gingipain domains than a corresponding group with healthy periodontium. Titers were predominantly directed toward the carbohydrate epitopes shared between the gingipains and the lipopolysaccharide ofP. gingivaliswith little recognition of the peptide backbone of the catalytic domains. Distribution of titers to peptide epitopes of the adhesin domains was as follows: HA4 ≈ HA1 > HA3 ≫ HA2. No correlation was observed between markers of disease severity and titers to individual adhesins within the disease group. Posttreatment titers showed no change or a decrease in titers for the majority of patients except for titers to the HA2 domain which showed marked increases in a few responding patients. Since the HA2 domain is important in hemoglobin binding and acquisition of essential porphyrin, boosting titers of antibodies to this domain may have the potential to control the growth of this organism.
