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Women are more susceptible to malaria during pregnancy due to malaria\u2010induced inflammation and the sequestration of infected red blood cells in the placenta, which bind to the chondroitin sulfate portion of syndecan\u20101 on the syncytiotrophoblast and in the intervillous space. Syndecan\u20101 is a dimeric proteoglycan with an extracellular ectodomain that is cleaved from the transmembrane domain (referred to as \u201cshedding\u201d) by matrix metalloproteinases (MMPs), likely the secreted MMP\u20109. The ectodomain includes four binding sites for chondroitin sulfate, which are proximal to the transmembrane domain, and six distal binding sites primarily for heparan sulfate. This \u201cshedding\u201d of syndecan\u20101 is inhibited by the presence of the heparan sulfate chains, which can be removed by heparanase. The intervillous space contains fibrin strands and syndecan\u20101 ectodomains free of heparan sulfate. The following is proposed as the sequence of events that leads to and is primarily responsible for sequestration in the intervillous space of the placenta. Inflammation associated with malaria triggers increased heparanase activity that degrades the heparan sulfate on the membrane\u2010bound syndecan\u20101. Inflammation also upregulates MMP\u20109 and the removal of heparan sulfate gives MMP\u20109 access to cleave syndecan\u20101, thereby releasing dimeric syndecan\u20101 ectodomains with at least four chondroitin sulfate chains attached. These multivalent ectodomains bind infected RBCs together leading to their aggregation and entrapment in intervillous fibrin. This mechanism suggests possible new targets for anti\u2010placental malaria drugs such as the inhibition of MMP\u20109. 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