Cysteine biosynthesis in Neisseria species

<jats:p>The principal mechanism of reducing sulfur into organic compounds is via the synthesis of <jats:sc>l</jats:sc>-cysteine. Cysteine is used for protein and glutathione synthesis, as well as being the primary sulfur source for a variety of other molecules, such as biotin, coenzyme A, lipoic acid and more. Glutathione and other cysteine derivatives are important for protection against the oxidative stress that pathogenic bacteria such as <jats:italic>Neisseria gonorrhoeae</jats:italic> and <jats:italic>Neisseria meningitidis</jats:italic> encounter during infection. With the alarming rise of antibiotic-resistant strains of <jats:italic>N. gonorrhoeae</jats:italic>, the development of inhibitors for the future treatment of this disease is critical, and targeting cysteine biosynthesis enzymes could be a promising approach for this. Little is known about the transport of sulfate and thiosulfate and subsequent sulfate reduction and incorporation into cysteine in <jats:italic>Neisseria</jats:italic> species. In this review we investigate cysteine biosynthesis within <jats:italic>Neisseria</jats:italic> species and examine the differences between species and with other bacteria. <jats:italic>Neisseria</jats:italic> species exhibit different arrangements of cysteine biosynthesis genes and have slight differences in how they assimilate sulfate and synthesize cysteine, while, most interestingly, <jats:italic>N. gonorrhoeae</jats:italic> by virtue of a genome deletion, lacks the ability to reduce sulfate to bisulfide for incorporation into cysteine, and as such uses the thiosulfate uptake pathway for the synthesis of cysteine.</jats:p>