Chang Arthur, Kaur Ravinder, Michel Lea Vacca, Casey Janet R, Pichichero Michael
Rochester General Hospital, Rochester General Research Institute, Center for Infectious Diseases and Immunology, Rochester, NY, USA.
Hum Vaccin. 2011 Jan 1;7(1):102-5. doi: 10.4161/hv.7.1.13351.
An outer membrane protein of nontypeable Haemophilus influenzae (NTHi), P6, is a vaccine candidate because it has been characterized as conserved among all H. influenzae strains. Among 151 isolates from children, age 6 to 30 months, evaluating NTHi nasopharyngeal (NP) and oropharyngeal (OP) colonization and tympanocentesis confirmed acute otitis media we identified 14 strains (9.3%) that had variant protein sequences of P6. One atypical omp P6 isolate had sequence mutations in the binding site of a proposed major antigenic epitope of omp P6 identified by monoclonal antibody 7F3. Eight strains (5.3%) had non-homologous variations in amino acids that could result in significant changes to the protein structure of P6, and 5 other strains had amino acid substitutions at four previously described key residue sites. These results show that NTHi omp P6 is not invariant in its structure among respiratory isolates from children.
不可分型流感嗜血杆菌（NTHi）的外膜蛋白P6是一种疫苗候选物，因为它在所有流感嗜血杆菌菌株中具有保守性。在对6至30个月大儿童的151株分离株进行评估时，这些分离株涉及NTHi鼻咽（NP）和口咽（OP）定植以及鼓膜穿刺确诊的急性中耳炎，我们鉴定出14株（9.3%）具有P6蛋白序列变异的菌株。一株非典型的omp P6分离株在单克隆抗体7F3鉴定的omp P6主要抗原表位的结合位点存在序列突变。8株（5.3%）在氨基酸上存在非同源变异，这可能导致P6蛋白结构发生显著变化，另外5株在四个先前描述的关键残基位点存在氨基酸替换。这些结果表明，NTHi omp P6在儿童呼吸道分离株中的结构并非一成不变。
