This study aimed to characterize matrix assembly mechanisms on the surface of the human pathogen Streptococcus pyogenes. Among 125 S. pyogenes isolates, 61% were able to recruit collagen type IV via surface‐bound fibronectin. Streptococcus gordonii expressing the fibronectin‐binding repeat domain of S. pyogenes SfbI protein was equally potent in recruiting collagen, indicating that this domain was sufficient to promote fibronectin‐mediated collagen recruitment. Electron microscopic analysis of streptococci revealed that fibronectin‐mediated collagen recruitment led to matrix deposition on and between streptococcal cells, which induced the formation of large bacterial aggregates. Furthermore, collagen‐recruiting streptococci were able to colonize collagen fibres and were protected from adhering to human polymorphonuclear cells in the presence of op‐sonizing antibodies. Fibronectin‐mediated collagen recruitment thus represents a novel aggregation, colonization and immune evasion mechanism of S. pyogenes.