菌株名称：伴放线放线杆菌 Aggregatibacter actinomycetemcomitans
其它编号：ATCC 29523
培养物和冻干菌种应在2-8℃保存，勿长期置于室温。
血平板培养基（TSA+5%脱纤维蛋白羊血）
培养条件：37℃ 5% CO2环境下培养
培养时间：48h
1、冻干粉复苏时全部用完，不得保留。
2、参照“开管说明”，用无菌吸管吸取0.3-0.5ml的培养液或者无菌水，滴入
冻干管中，轻轻振荡至其溶解。吸取全部菌悬液，接种在培养基上(建议不超过
2个平板)。
3、经过冷冻干燥保藏，菌种处于休眠状态，复苏培养时可能会延迟生长，这时需
较长的培养时间。
4、请将实验废弃物高温高压灭菌处理后再作丢弃。
5、若您收到的是已复苏的培养物(非冻干菌)，则可以直接用于您的实验，或根
据需要转接培养。
Aggregatibacter actinomycetemcomitans is a Gram-negative, facultative anaerobe, nonmotile bacterium that is often found in association with localized aggressive periodontitis, a severe infection of the periodontium. It is also suspected to be involved in chronic periodontitis. Less frequently, A. actinomycetemcomitans is associated with nonoral infections such as endocarditis. Its role in aggressive periodontitis was first discovered by Danish-born periodontist Jørgen Slots, a professor of dentistry and microbiology at the University of Southern California School of Dentistry.
'Bacterium actinomycetem comitans' was first described by Klinger (1912) as coccobacillary bacteria isolated with Actinomyces from actinomycotic lesions in humans. It was reclassified as Actinobacillus actinomycetemcomitans by Topley & Wilson (1929) and as Haemophilus actinomycetemcomitans by Potts et al. (1985). The species has attracted attention because of its association with localized aggressive periodontitis.
It is one of the bacteria that might be implicated in destructive periodontal disease. Although it has been found more frequently in localized aggressive periodontitis, prevalence in any population is rather high. It has also been isolated from actinomycotic lesions (mixed infection with certain Actinomyces species, in particular A. israelii). It possesses certain virulence factors that enable it to invade tissues, such as the pore-forming toxin leukotoxin A. It has also been isolated from women with bacterial vaginosis and as an etiologic agent in endocarditis.[4] The pore-forming toxin LtxA of A. actinomycetemcomitans may be a trigger of the autoimmune disease rheumatoid arthritis due to its ability to stimulate protein citrullination, a post-translational protein modification targeted by autoantibodies in this disease.
