There are two surface glycoproteins expressed in Influenza that both express N-linked oligosaccharides,

hemagglutinin (HA) and neuraminidase (NA). N-linked glycosylation is a frequent post-translational

alteration of glycoproteins via oligosaccharides (carbohydrates) are bound by N-glycosidic connections
to the Asn residue Asn-X-Ser/Thr -X (X can be any amino acid but proline). N-linked glycosylation of the
HA and NA arises in the endoplasmic reticulum and Golgi apparatus just like host cell glycoproteins.
Glycans expressed at glycolysation sites on HA and NA are controlled by the host cell and the existing
processing between cells. HA and NA can have a combination of high-mannose (branches ending in the
sugar mannose), complex (branches ending in the galactose or GalNAc), or a mixture of
oligosaccharides. Influenza N-linked glycans in HA can be enzyme-catalyzed conjugated to a sulfo group
to change its structure. Complex glycans expressed by HA do not have sialic acid, as it is cleaved by NA.
N-linked glycosylation is repressed by amalgamations of Asn-X-Ser (X being again any amino acid but
proline) or the glycosylation motif is followed by particular sequences such as Asn-X-Ser/Thr-Trp or Asn-
X-Ser/Thr-Glu.

Tate, M., Job, E., Deng, Y.-M., Gunalan, V., Maurer-Stroh, S., & Reading, P. (2014). Playing Hide and Seek:
How Glycosylation of the Influenza Virus Hemagglutinin Can Modulate the Immune Response to
Infection. Viruses, 6(3), 1294–1316. https://doi.org/10.3390/v6031294