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Interaction between a Chlamydia trachomatis inclusion membrane protein (Inc) and host cell 14-3-3 proteins
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Resumo(s)
Chlamydia trachomatis is an obligate intracellular bacterium that causes genital and ocular infections
in humans. Its multiplication in host cells occurs exclusively inside a membrane-bound compartment,
known as inclusion. To enter, multiply and exit host cells, C. trachomatis transports proteins through a
type III secretion system into the host cell. These proteins include Incs, which insert into the inclusion
membrane, modifying it, and manipulating the host cell in various ways. In this work, the interaction of
an Inc protein (CT006) from C. trachomatis with 14-3-3 proteins of the host cell was studied. There are
seven isoforms of 14-3-3 proteins known in mammals that in general have the capacity to bind to several
signaling proteins, being able to regulate several cellular processes. It was observed that all 14-4-3
isoforms (β/ε/η/γ/σ/τ/ζ) are recruited to the periphery of the inclusion membrane, probably in an Inc
CT006-independent-manner, but only 14-3-3β/η/γ/σ interact with Inc CT006. By analyzing the primary
structure of Inc CT006 it was realized that although the protein has potential 14-3-3 binding motifs, none
seems to be exclusively necessary for the interaction. However, any one of the motifs when present
and active can promote the interaction. 14-3-3 proteins are also thought to interact with Inc CT006
through their conserved binding groove. In summary, this work supports the idea that 14-3-3 proteins
have a relevant role in the intracellular multiplication of C. trachomatis. Future studies with C.
trachomatis with the gene encoding Inc CT006 inactivated or overexpressed, and/or with host cell with
reduced levels of 14-3-3 proteins, might clarify how the interaction of Inc CT006 with 14-3-3 proteins
contribute to the intracellular multiplication of C. trachomatis.
Descrição
Palavras-chave
Chlamydia trachomatis Inc CT006 14-3-3 proteins protein-protein interaction