Extraintestinal pathogenic Escherichia coli (ExPEC) is an important
zoonotic pathogen that places severe burdens on public
health and animal husbandry. There are many pathogenic
factors in E. coli. The type VI secretion system (T6SS) is a
nano-microbial weapon that can assemble quickly and inject
toxic effectors into recipient cells when danger is encountered.
T6SSs are encoded in the genomes of approximately
25% of sequenced Gram-negative bacteria. When these bacteria
come into contact with eukaryotic cells or prokaryotic
microbes, the T6SS assembles and secretes associated effectors.
In the porcine ExPEC strain PCN033, we identified four
classic rearrangement hotspot (Rhs) genes. We determined
the functions of the four Rhs proteins through mutant construction
and protein expression. Animal infection experiments
showed that the Δrhs-1CT, Δrhs-2CT, Δrhs-3CT, and
Δrhs-4CT caused a significant decrease in the multiplication
ability of PCN033 in vivo. Cell infection experiments showed
that the Rhs protein is involved in anti-phagocytosis activities
and bacterial adhesion and invasion abilities. The results
of this study demonstrated that rhs1, rhs3, and rh4 plays an
important role in the interaction between PCN033 and host
cell. Rhs2 has contribution to cell and mice infection. This
study helps to elucidate the pathogenic mechanism governing
PCN033 and may help to establish a foundation for further
research seeking to identify potential T6SS effectors.
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