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GapA-1 has previously been shown to be up-regulated on bacterial contact with host epithelial cells and is accessible to antibodies on the surface of capsule-permeabilized meningococcal cells. The aims of this study were: 1) to determine whether GapA-1 was expressed across different strains of <jats:italic>N. meningitidis<\/jats:italic>; 2) to determine whether GapA-1 surface accessibility to antibodies was dependant on the presence of capsule; 3) to determine whether GapA-1 can influence the interaction of meningococci and host cells, particularly in the key stages of adhesion and invasion.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>In this study, expression of GapA-1 was shown to be well conserved across diverse isolates of <jats:italic>Neisseria<\/jats:italic> species. Flow cytometry confirmed that GapA-1 could be detected on the cell surface, but only in a <jats:italic>siaD<\/jats:italic>-knockout (capsule-deficient) background, suggesting that GapA-1 is inaccessible to antibody in <jats:italic>in vitro<\/jats:italic>-grown encapsulated meningococci. The role of GapA-1 in meningococcal pathogenesis was addressed by mutational analysis and functional complementation. Loss of GapA-1 did not affect the growth of the bacterium <jats:italic>in vitro<\/jats:italic>. However, a GapA-1 deficient mutant showed a significant reduction in adhesion to human epithelial and endothelial cells compared to the wild-type and complemented mutant. A similar reduction in adhesion levels was also apparent between a <jats:italic>siaD<\/jats:italic>-deficient meningococcal strain and an isogenic <jats:italic>siaD gapA-1<\/jats:italic> double mutant.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>Our data demonstrates that meningococcal GapA-1 is a constitutively-expressed, highly-conserved surface-exposed protein which is antibody-accessible only in the absence of capsule. Mutation of GapA-1 does not affect the <jats:italic>in vitro<\/jats:italic> growth rate of <jats:italic>N. meningitidis<\/jats:italic>, but significantly affects the ability of the organism to adhere to human epithelial and endothelial cells in a capsule-independent process suggesting a role in the pathogenesis of meningococcal infection.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2180-10-280","type":"journal-article","created":{"date-parts":[[2010,11,9]],"date-time":"2010-11-09T19:24:20Z","timestamp":1289330660000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":71,"title":["The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells"],"prefix":"10.1186","volume":"10","author":[{"given":"Sarfraz A","family":"Tunio","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neil J","family":"Oldfield","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dlawer AA","family":"Ala'Aldeen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl G","family":"Wooldridge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David PJ","family":"Turner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2010,11,9]]},"reference":[{"issue":"Suppl 2","key":"1236_CR1","doi-asserted-by":"publisher","first-page":"B64","DOI":"10.1016\/j.vaccine.2009.04.061","volume":"27","author":"DA Caugant","year":"2009","unstructured":"Caugant DA, Maiden MCJ: Meningococcal carriage and disease - population biology and evolution. 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