MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Role of sialic acid-containing glycans of matrix metalloproteinase-9 (MMP-9) in the interaction between MMP-9 and staphylococcal superantigen-like protein 5. Role of sialic acid-containing glycans of matrix metalloproteinase-9 (MMP-9) in the interaction between MMP-9 and staphylococcal superantigen-like protein 5. Microbiology and immunology 2018 imex curation Kurisaka C., Oku T., Itoh S., Tsuji T. tsuji@hoshi.ac.jp 13-Nov-2020: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Kurisaka C., Oku T., Itoh S., Tsuji T. tsuji@hoshi.ac.jp Accepted 2020-SEP-30 AT 10:36 BST AT 10:36 BST by KALPANAP Microbiology and immunology 2018 Only protein-protein interactions imex curation imex curation mmp9_human Matrix metalloproteinase-9 MMP9 CLG4B 92 kDa type IV collagenase 92 kDa gelatinase Gelatinase B protein protein human Homo sapiens Human MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED DIP protein P14780 original sequence version: 114 DIP protein P14780 original sequence version: 120 2165AC8CA1466209 q9zfs6_staau set3 NCTC7878_00467 FPP26_02070 protein protein staau Staphylococcus aureus MKMTAIAKASLALSILATGVITSTAQTVNASEHESKYENVTKDIFDLRDYYSRASKELKNVTGYRYSKGGKHYLIFDKNRKFTRIQIFGKDIERIKKRKNPGLDIFVVKEAENRNGTVYSYGGVTKKNQGAYYDYLSAPRFVIKKEVGAGVSVHVKRYYIYKEEISLKELDFKLRQYLIQDFDLYKKFPKASKIKVTMKDGGYYTFELNKKLQTNRMSDVIDGRNIEKIEANIR E488C0EC35E1AE67 mmp9-4 1 2 unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level human-thp-1 Homo sapiens acute monocytic leukemia cells thp-1 Human acute monocytic leukemia cell line 3 unspecified role unspecified role bait bait purified purified GST tag GST tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association f2a f4b f5 f7b he pull‐down assay using GST‐SSL5‐agarose in combination with zymography or western blotting showed that immobilized SSL5 bound to MMP‐9 derived from CHO‐K1 cells but did not bind to MMP‐9 from Lec2 mutant cells (Fig. 5). Pull‐down assay clearly showed that GST‐SSL5‐agarose failed to coprecipitate neuraminidase‐treated MMP‐9 (Fig. 4b). The pull‐down assay with GST‐SSL5‐agarose showed that MMP‐9 from benzyl‐GalNAc‐treated THP‐1 cells possessed weaker reactivity with GST‐SSL5 (Fig. 7b), suggesting that O‐gycans of MMP‐9 play a crucial role in its binding to GST‐SSL5. set3-mmp9-1 1 2 unspecified role unspecified role prey prey purified purified human-thp-1 Homo sapiens acute monocytic leukemia cells thp-1 Human acute monocytic leukemia cell line 3 unspecified role unspecified role bait bait purified purified GST tag GST tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction f6b The pull‐down assay showed that both the intact and de‐N‐glycosylated MMP‐9 were similarly coprecipitated with GST‐SSL5‐agarose (Fig. 6b).