Lineage structure of Streptococcus pneumoniae may be driven by immune selection on the groEL heat-shock protein

Sci Rep. 2017 Aug 22;7(1):9023. doi: 10.1038/s41598-017-08990-z.

Abstract

Populations of Streptococcus pneumoniae (SP) are typically structured into groups of closely related organisms or lineages, but it is not clear whether they are maintained by selection or neutral processes. Here, we attempt to address this question by applying a machine learning technique to SP whole genomes. Our results indicate that lineages evolved through immune selection on the groEL chaperone protein. The groEL protein is part of the groESL operon and enables a large range of proteins to fold correctly within the physical environment of the nasopharynx, thereby explaining why lineage structure is so stable within SP despite high levels of genetic transfer. SP is also antigenically diverse, exhibiting a variety of distinct capsular serotypes. Associations exist between lineage and capsular serotype but these can be easily perturbed, such as by vaccination. Overall, our analyses indicate that the evolution of SP can be conceptualized as the rearrangement of modular functional units occurring on several different timescales under different pressures: some patterns have locked in early (such as the epistatic interactions between groESL and a constellation of other genes) and preserve the differentiation of lineages, while others (such as the associations between capsular serotype and lineage) remain in continuous flux.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Capsules / genetics
  • Bacterial Capsules / immunology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / immunology
  • Biological Evolution
  • Chaperonin 60 / genetics*
  • Chaperonin 60 / immunology
  • Epistasis, Genetic
  • Machine Learning
  • Operon
  • Serotyping
  • Streptococcus pneumoniae / genetics
  • Streptococcus pneumoniae / immunology*

Substances

  • Bacterial Proteins
  • Chaperonin 60