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Here, we demonstrate that when the obligate intracellular parasite\n                      <jats:italic toggle=\"yes\">Toxoplasma gondii<\/jats:italic>\n                      secretes its rhoptry organelle contents into the host cytoplasm before invasion\u2014a process called \u201ckiss and spit\u201d\u2014host cell metabolite abundance is altered in nucleotide synthesis, the pentose phosphate pathway, glycolysis, and amino acid synthesis. U-13C6-labeling metabolomics confirmed that kiss and spit increased the flow of carbon through the pentose phosphate pathway and nucleotide synthesis. An increase in 2,3-bisphosphoglycerate abundance led us to investigate the activation of host cytosolic nucleosidase II (cN-II) to provide purines for the parasite. We found that\n                      <jats:italic toggle=\"yes\">T. gondii<\/jats:italic>\n                      manipulates the host cN-II enzyme to dephosphorylate GMP and IMP that it needs for replication. Furthermore, we found that the approved anti-cancer drug fludarabine, which inhibits cN-II, also inhibits\n                      <jats:italic toggle=\"yes\">Toxoplasma<\/jats:italic>\n                      replication. These results reveal\n                      <jats:italic toggle=\"yes\">Toxoplasma<\/jats:italic>\n                      host cell manipulation and highlight potential therapies for toxoplasmosis.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        A fundamental challenge in parasitology is understanding how intracellular parasites rapidly reprogram host metabolism to support replication. This study reveals that\n                        <jats:italic toggle=\"yes\">Toxoplasma gondii<\/jats:italic>\n                        initiates profound metabolic reprogramming through a \u201ckiss-and-spit\u201d mechanism, secreting effector molecules without invasion. We demonstrate that\n                        <jats:italic toggle=\"yes\">T. gondii<\/jats:italic>\n                        specifically hijacks host cytosolic 5\u2032-nucleotidase II (cN-II) by elevating 2,3-bisphosphoglycerate levels, which allosterically activates this enzyme to generate purines essential for parasite survival. Genetic deletion of host cN-II significantly impairs parasite replication, establishing cN-II as a critical host dependency factor. These findings have important implications for antiparasitic drug development while advancing our understanding of purine metabolism in apicomplexan parasites. More broadly, elucidating the molecular mechanism linking parasite effector secretion to specific host enzyme activation provides a framework for understanding metabolic manipulation across other intracellular pathogens.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/msphere.00256-26","type":"journal-article","created":{"date-parts":[[2026,6,15]],"date-time":"2026-06-15T12:02:01Z","timestamp":1781524921000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Kiss and spit metabolomics highlight the role of host purine metabolism during pathogen infection"],"prefix":"10.1128","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7872-5595","authenticated-orcid":true,"given":"Gina 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